ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (363)
  • Wiley-Blackwell  (363)
  • Periodicals Archive Online (PAO)
  • 1985-1989  (363)
  • 1960-1964
  • 1955-1959
  • 1950-1954
Collection
Keywords
Publisher
  • Wiley-Blackwell  (363)
  • Periodicals Archive Online (PAO)
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Chelonus sp. near curvimaculatus venom proteins: Analysis of their potential role and processing during development of host Trichoplusia ni (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 1-12 
    Details
    ISSN: 0739-4462
    Keywords: Chelonus ; venom proteins ; parasitization ; Trichoplusia ni ; venom antiserum ; parasite oviposition ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The venom that Chelonus sp. near curvimaculatus injects into each parasitized Trichoplusia ni egg is entirely injected within the first 8 s of the 19-s oviposition period, before deposition of the parasitoid egg that is injected during the final 1-2 s of the oviposition. The parasitization factor, causing precocious metamorphosis of the host, is injected after the venom, but before the parasite egg. The venom by itself does not cause developmental redirection of the host. Chelonus venom proteins are very stable in the host egg during the first 2 days of egg development. Then, on the last day before hatching, they are rapidly degraded by the proteolytic enzymes appearing in 3-day-old T. ni eggs. Among those that degrade the venom proteins are serine-type proteinases, and at least one seems to be a trypsin-like enzyme.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100102
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Canalization of the redbanded leafroller mothArgyrotaenia velutinana (Walker), Lepidoptera: Tortricidae. sex pheromone blend (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 73-82 
    Details
    ISSN: 0739-4462
    Keywords: Argyrotaenia velutinana ; selection ; (E)-11-tetradecenyl acetate ; (E)-9-dodecenyl acetate ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Previous attempts to shift the (Z)-11-/(E)-11-tetradecenyl acetate ratio of pheromone components in the redbanded leafroller moth (RBLR), Argyrotaenia velutinana, by several selection protocols showed that this ratio is strongly canalized. Analysis of the complete seven-component blend, however, showed that a Geneva laboratory stock of RBLR had a lower percent (20%) of the E9-12:OAc minor component compared to the E11-14:OAc component than a population of RBLR from North Carolina (31%). Hybrid populations from these two cultures were used in a two-way family truncation selection scheme in which families were selected for either the lowest (low line) or the highest (high line) ratio of E9-12:OAc/E11-14:OAc. After three generations of selection, the low line had 14% E9-12:OAc relative to E11-14:OAc and the high line had 42%. The selection pressure was removed in generations 4-9, and the low line remained unchanged at 14% E9-12:OAc; but in the high line, it drifted to 53%.Studies were conducted to estimate heritability and realized heritability. The realized heritability calculated for each generation of selection averaged 1.14 for the low line and 1.50 for the high line. These calculations, along with estimated heritability values of 0.416 and 0.644 for reciprocal crosses, indicate some plasticity in the E9-12:OAc/E11-14:OAc ratio. This ratio was positively correlated to the total amount of 12-carbon components to 14-carbon components, but was negatively correlated to the Z/E ratio of Δ11-tetradecenylacetates.The results of two studies on the canalization of various components of the RBLR sex pheromone blend indicate that there is limited potential in this insect for manipulation of the blend ratios in the laboratory.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100107
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Storage proteins of the fall webworm, Hyphantria cunea drury (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 115-130 
    Details
    ISSN: 0739-4462
    Keywords: hemolymph ; fat body ; yolk protein ; vitellogenin ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Two storage proteins, storage protein-1 (SP1) and storage protein-2 (SP2), were found in hemolymph and fat body during the development of Hyphantria cunea, the fall webworm. Both storage proteins show similiar quantitative changes during development in males and females; however, SP1 is more abundant. The hemolymph of last instar larvae contains high concentrations of the storage proteins. However, following pupation, the storage proteins accumulate in fat bodies. SP1 peaks in the hemolymph of males and females late in last instar larvae (8-day-old 7th instar larvae).SP1 has a native molecular weight of 460,000 and consists of six identical subunits (Mr = 76,700), while SP2 has a molecular weight of 450,000 and is composed of two different subunits (Mr = 74,100 and 72,400). Both SP1 and SP2 are hexamers and are phosphorylated glycolipoproteins. The pl values of SP1 and SP2 were determined to be 5.70 and 5.50, respectively.Antibodies raised against SP1 react positively with vitellogenin and ovary extract, as well as with proteins in the hemolymph from last instar larvae and proteins in pupal fat bodies. Storage protein synthesis starts in fat bodies of a 4-day-old 7th instar larvae and in female peaks at 6-8 days of the 7th instar.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100203
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Sex pheromone blend of Manduca sexta: Responses of central olfactory interneurons to antennal stimulation in male moths (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 281-291 
    Details
    ISSN: 0739-4462
    Keywords: antennal lobe ; electrophysiology ; olfaction ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Recently, chemical analysis of solvent rinses of the external surfaces of pheromone glands from female Manduca sexta revealed a blend of 12 aldehydes, including the previously identified sex pheromone component, (E,Z)-10,12-hexadecadienal (bombykal). Previous electrophysiological studies showed that olfactory (deutocerebral) interneurons in the antennal lobes of males exhibited a wide range of responsiveness to pheromonal stimulation of the ipsilateral antenna. These experiments were performed with crude extracts of pheromone glands as well as two synthetic compounds: the major pheromone component, bombykal, and (E,Z)-11,13-pentadecadienal, a mimic of a second component of the female's pheromone blend. Using intracellular methods, we have now reexamined similar olfactory interneurons, using each of the 12 chemically identified components as well as synthetic blends of various combinations of them. Eight of the 12 components isolated from female glands elicited some form of response in olfactory interneurons in males. In accordance with biochemical and behavioral data, the most potent are bombykal and two trienals, (E,E,E)- and (E,E,Z)-10,12,14-hexadecatrienal. We also conclude that the C15 dienal is selective for one of the trienal receptors on the antenna, but is much less potent than the natural trienal stimulant.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100404
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110101
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Some macromolecular abnormalities developed by the interaction of malathion and permethrin and subsequent refeeding in Tribolium castaneum larvae (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 203-215 
    Details
    ISSN: 0739-4462
    Keywords: acetylcholine esterase ; protein ; carbohydrate-metabolizing enzymes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The effects of sublethal treatments of malathion and malathion + permethrin combinations on activities of acetylcholine esterase (ChE), carbohydrate-metabolizing enzymes (amylase; lactate dehydrogenase, LDH), protein-metabolizing enzymes (alanine and aspartate aminotransferase, ALAT, ASAT), as well as acid and basic phosphatases (AcP and AkP, respectively), and Kreb's cycle enzymes (isocitrate dehydrogenase, ICDH) were studied on sixth instar larvae of the red flour beetle, Tribolium castaneum. In addition, the levels of lipid, cholesterol, glucose, glycogen, proteins, free amino acids (FAA), urea, and nucleic acids (DNA and RNA) were determined. Malathion (400 ppm) increased the activity of LDH (53%), as well as the concentrations of FAA (31%) and urea (39%). Malathion treatments of 400 ppm decreased the glucose (20%) and glycogen (24%) content but did not affect other enzymes and biochemical components. Permethrin (200 ppm) and malathion (20 ppm) mixtures increased the activities of ChE (708%) and LDH (55%), and raised the concentrations of FAA (26%), urea (24%), glucose (23%), lipid (14%), cholesterol (21%), DNA (24%), and RNA (8%). The decrease in AcP activity and in glycogen concentration observed with malathion was sustained by permethrin in the mixture. Permethrin + malathion mixtures also depressed the levels of AkP (30%), ICDH (24%), and glycogen (36%). The intensity of effects commensurated with the dose and duration of insecticide exposure. Refeeding showed tendencies towards normalization of various biochemical parameters.
    Additional Material: 7 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110402
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Stimulating action of methyl 12, 12, 12-trifluorofarnesoate on in vitro juvenile hormone III biosynthesis in blattella germanica (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 257-270 
    Details
    ISSN: 0739-4462
    Keywords: German cockroach ; corpora allata ; farnesoic acid ; 12, 12, 12-trifluorofarnesoic acid ; 12, 12, 12-trifluorofarnesol ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Methyl 12, 12, 12-trifluorofarnesoate (MTFF) at a dose of 10 μM, stimulated in vitro juvenile hormone (JH) release in corpora allata (CA) from 6-day-old, freshly ecdysed, and 8-day-old (period of ootheca transport) adult virgin females of Blattella germanica. In addition, MTFF also induced intraglandular accumulation of JH and MF in treated CA. Trifluorofarnesoic acid (TFFA) and trifluorofarnesol (TFF) exhibited the same properties, although to a lesser extent than MTFF. The detection of MTFF in TFFA-treated CA suggested that TFFA and TFF were biotransformed into MTFF by the CA enzymatic system and that this ester might be responsible for the activity observed. Equivalent experiments carried out with farnesoic acid (FA) resulted in a more significant stimulation of JH production. This is not surprising, because exogenous FA is readily epoxidized at C10-C11 double bond and methylated to afford JH. Conversely, analytical data have shown that the C6-C7 double bond of MTFF is epoxidized by the CA enzymatic system, whereas that at C10-C11 remains practically unaltered.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110406
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Microplitis croceipes teratocytes cause developmental arrest of Heliothis virescens larvae (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 51-61 
    Details
    ISSN: 0739-4462
    Keywords: tobacco budworm ; Braconidae ; trophoserosa cells ; juvenile hormone esterase ; polydnavirus ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Microplitis croceipes teratocytes placed into nonparasitized Heliothis virescens larvae survived in the absence of a parasitoid larva and caused developmental changes in the host. Expressions of these changes included delayed larval mortality, incomplete larval-pupal ecdysis, or delayed pupation. Two day old 4th stadium H. virescens larvae were more sensitive to injected teratocytes than were 5th stadium larvae. Three day old teratocytes were more effective than were 6 day old teratocytes. The degree of response was related to the number of injected teratocytes. For example, 750 three day old teratocytes (the approximate number from a single parasitoid egg) caused delayed larval mortality in 96% of the treated larvae whereas 175 three day old teratocytes caused delayed larval mortality in only 33% of the treated larvae. Even a dose of 80 teratocytes resulted in 15% incomplete larval-pupal ecdysis compared to 0% for controls. Treatment with hemocyte-and teratocyte-free hemolymph from parasitized larvae, hemocytes from nonparasitized H. virescens, unfertilized M. croceipes eggs, Cotesia congregata teratocytes, or Micrococcus lysodeikticus cells all had very little effect either on larval growth or development time.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120105
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Relationship between the fatty acids of fat body triacylglycerol and lipophorin diacylglycerol of non-diapause and diapause larvae of the southwestern corn borer, Diatraea grandiosella (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 123-131 
    Details
    ISSN: 0739-4462
    Keywords: larval diapause ; juvenile hormone analog ; hemolymph ; palmitate ; palmitoleate ; oleate ; linoleate ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The fatty acids of the triacylglycerol reserves in the fat body and of the diacylglycerol of lipophorin in the hemolymph of non-diapause and diapause larvae of D. grandiosella were compared. For both non-diapause and diapause larvae palmitate, palmitoleate, oleate, and linoleate were the predominant fatty acids present in fatty body triacylglycerol, and palmitate, oleate, and linoleate were the predominant fatty acids present in lipophorin diacylglycerol. However, differences were detected in the relative amounts of oleate and linoleate present in lipophorin diacylglycerol of non-diapause and diapause larvae. The relative amount of linoleate in lipophorin diacylglycerol declined during diapause, whereas that of oleate remained relatively high during diapause. The fatty acid profile of lipophorin diacylglycerol from non-diapause larvae treated with a juvenile hormone analog to induce a diapause-like state more closely matched that of diapause larvae than that of non-diapause larvae. The differences detected in the fatty acid composition of lipophorin diacylglycerol in non-diapause and diapause larvae appear to be due mainly to the different physiological states rather than to the different rearing temperatures employed. The results are discussed in relation to the essential role fatty acids, especially oleate, play in the survival of diapause larvae.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120206
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Degradation of juvenile hormone and methylation of juvenile hormone acid by corpora cardiaca-corpora allata of the cockroach, Nauphoeta cinerea: I. Biochemical aspects (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 303-316 
    Details
    ISSN: 0739-4462
    Keywords: juvenile hormone metabolites ; L-[14C]methionine incorporation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Corpora cardiaca-corpora allata (CC-CA) from vitellogenic females of Nauphoeta cinerea degraded, in vitro, racemic and (10R)-juvenile hormone III (JH III) at a rate of 249 pmol/CC-CA/h and 786 pmol/CC-CA/h, respectively. The major metabolite formed was JH III acid, together with some highly polar products. CC-CA homogenates degraded racemic JH III to a small extent, whereas (10R)-JH III was degraded efficiently to JH III acid. No highly polar products were formed by CC-CA homogenates. When CC-CA were incubated with racemic JH III acid, some of this substance was degraded to highly polar products, and a minor part was methylated to JH III. CC degraded very little JH III acid and did not methylate it to JH III. CC-CA homogenates methylated JH III acid very efficiently; we measured an apparent Kmax of 37.8 μM and a Vmax of 1,260 pmol/4 h/ CC-CA equivalent. The addition of JH III acid to CC-CA in vitro increased the rate of biosynthesis of JH III, as determined by measuring incorporation of methyl[14C]methionine into JH III. These data indicate that the metabolite JH III acid can enter the CA and be methylated to JH III.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100406
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 11
    Electronic Resource
    Electronic Resource
    Ecdysteroids from developing eggs of Pieris brassicae (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 1-11 
    Details
    ISSN: 0739-4462
    Keywords: cholesterol ; ecdysone ; 20-hydroxyecdysone ; 26-hydroxyecdysone ; 20,26-dihydroxyecdysone ; ecdysonoic acid ; 20-hydroxyecdysonoic acid ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Ecdysone metabolism in Pieris brassicae eggs was revealed after injection of [3H]ecdysone into eggs. Labeled ecdysteroids were analyzed by HPLC. The metabolic fate of [3H]ecdysone is similar to that observed during postembryonic development, i.e., the larval instars and pupal instar. The ecdysone molecule is affected by hydroxylations at C-20 and at C-26; 26-hydroxyecdysteroids can be further oxidized into ecdysteroid acids. In an effort to identify egg ecdysteroids, we examined the metabolism of [3H]cholesterol injected into female pharate adults to achieve long-term labeling. In eggs, [3H]cholesterol was converted to 20-hydroxyecdysonoic acid, ecdysonoic acid, 20-hydroxyecdysone, and ecdysone. The rates of [3H]cholesterol incorporation into ecdysteroids increase according to the age of the eggs (from 0.06% at laying to 0.12% at hatching), while the cholesterol level remains constant throughout embryogenesis, suggesting that the embryos of Pieris brassicae can produce ecdysteroids either from cholesterol or from apolar ecdysteroids not identified by the analytical method. Pieris eggs contain amounts of ecdysteroids which increase from 1.5 nmol/g at laying to 3.8 nmol/g at hatching.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110102
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 12
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110201
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 13
    Electronic Resource
    Electronic Resource
    Ecdysone metabolism in the host-parasitoid-system Trichoplusia ni/Chelonus sp (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 79-92 
    Details
    ISSN: 0739-4462
    Keywords: ecdysteroids ; parasitization ; endysone ; parasites ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In unparasitized 4th and 5th-instar larvae of Trichoplusia ni and in 4th-instar larvae parasitized by Chelonus sp. 20-hydroxyecdysone, 20,26-dihydroxyec-dysone, and 20-hydroxyecdysonoic acid were the predominant metabolites formed 2 h after injection of [3H]ecdysone. Other unidentified metabolites were seen, but none seemed to be specific for either parasitized or unparasitized larvae. The major difference between parasitized and unparasitized larvae was seen with respect to the quantity of apolar (unidentified) and polar metabolites (20-hydroxyecdysonoic acid and unidentified ones), which were produced to a greater extent in parasitized larvae. Ecdysone was rapidly converted into 20-hydroxyecdysone and the other polar metabolites in all stages investigated, and the parasitoid seemed not to affect the conversion of ecdysone into 20-hydroxyecdysone. When analyzing the fate of [3H]ecdysone in host and parasite separately, at a stage when the parasite drinks hemolymph of its host, we observed that 10-20% of the radioactivity was recovered from the parasitoid. Analysis of the parasitoid's ecdysteroids revealed that ecdysone and 20-hydroxyecdysone represented only a small proportion of the recovered labeled ecdysteroids, the majority being apolar and polar metabolites. Our data suggest that the parasitoid takes up ecdysteroids from its host, converts them, and to some extent releases apolar metabolites into the host.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110203
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 14
    Electronic Resource
    Electronic Resource
    Chemical- and cuticular phenoloxidase- mediated synthesis of cysteinyl-catechol adducts (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 127-137 
    Details
    ISSN: 0739-4462
    Keywords: quinone tanning ; cuticular sclerotization ; amino acid-catechol adducts ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: N-Acetylcysteine adducts of o-benzoquinones derived from catechol, 4-methylcatechol, and N-acetyldopamine were chemically synthesized and characterized by a combination of UV, IR, and NMR spectral studies. Oxidation of catechol, 4-methylcatechol, and N-acetyldopamine by cuticle-bound phenoloxidase from Sarcophaga bullata in the presence of N-acetylcysteine resulted in the formation of covalent adducts between catecholic compounds and N-acetylcysteine. Structural identities of these adducts were established by comparison of their HPLC retention time and UV spectra with those of synthetic adducts and by cochromatography with authentic samples. Although insect cuticle is known to contain only trace amounts of cysteine, the in vitro synthesis of quinone cysteine adducts mediated by cuticular phenoloxidase strongly indicates the occurrence of similar reactions in vivo as well and is in support of Pryor's quinone tanning hypothesis.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110206
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 15
    Electronic Resource
    Electronic Resource
    A high molecular weight diapause-associated protein from the stem-borer Busseola fusca: Purification and properties (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 173-187 
    Details
    ISSN: 0739-4462
    Keywords: Busseola-diapause protein ; physical-chemical properties ; immunology ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The hemolymph of diapausing larvae of the stem borer, Busseola fusca Fuller (Lepidoptera: Noctuidae), contains an electrophoretically distinct protein band on nondenaturing polyacrylamide gels. The protein, called the Busseola diapause protein (BDP), was purified by a combination of density gradient ultracentrifugation, gel permeation, and affinity chromatography. It is a high molecular weight protein (Mr ∼5 × 105; pl = 6.1) that is composed of two subunits, I (Mr ∼88,000 ± 4,000) and II (Mr ∼79,000 ± 1,000), which are not linked by disulfide bridges. The protein contains both lipids (2%) as well as covalently bound carbohydrates (1%). The inability to stain the fluorescein isothiocyanate-conjugated concanavalin A (FITC-Con A) suggests that the carbohydrate moiety of BDP is not of the high mannose type. Amino acid analysis showed a high tyrosine plus phenylalanine content (16 mol%). Labeling studies using [35S]-methionine showed that de novo synthesis by the fat body tissue occurs only in diapausing larval insects. It is proposed that the BDP could serve a storage function by providing the amino acids needed for the synthesis of pupal and adult structures.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110305
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 16
    Electronic Resource
    Electronic Resource
    Meeting announcements (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 273-273 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110407
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 17
    Electronic Resource
    Electronic Resource
    Ovarian muscularis of the stable fly Stomoxys calcitrans: Its structural, motile, and pharmacological properties (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 15-30 
    Details
    ISSN: 0739-4462
    Keywords: ovarian motility ; impedance myographs ; actions of octopamine ; proctolin ; glutamate ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The muscles of the ovary of the stable fly (Stomoxys calcitrans) appear to consist of two groups: (1) a network of stellate muscle cells that cover the surface of the ovary and (2) fibers that surround the ovarioles. Innervation of the ovaries was largely restricted to the region of the pedicels. The structural arrangements of the ovarian muscles provided the basis for two distinct patterns of movement. The contraction of the sheath that surrounds the ovary produced the appearance of a pulsing sphere, while the activation of muscle fibers that encompass the ovarioles may cause a vertical translation of eggs within the tubes. The various patterns of motility derived from the combined and separate actions of these two groups of muscles are described. Oscillations in the size of the ovary were the most prominent and frequent kind of spontaneous activity observed. A complete cycle of oscillation ranged from 200 ms to 4 s. Day-old stable flies consistently had the highest rate (30%) of ovarian sheath compression of the three age groups examined, while 2-day-old flies had the lowest (less than 10%). Seven-day flies had inconsistent rates that ranged from o to 25%. Two kinds of ovarian compression were recognized on impedance myographs on the basis of small and large amplitudes. Changes in tonus were also detected. Octopamine produced large increases in the amplitude of spherical compressions at 10-7 M. The neuropeptide proctolin (10-9 M) caused changes in both the frequency and amplitude of ovarian contractions. Glutamic acid consistently caused a marked reduction in the amplitude of ovarian compressions.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120103
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 18
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120201
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 19
    Electronic Resource
    Electronic Resource
    Biosynthesis of sex pheromone components from linolenic acid in arctiid moths (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 89-97 
    Details
    ISSN: 0739-4462
    Keywords: Phragmatobia fuliginosa ; Estigmene acrea ; radiolabeled fatty acids ; elongationdecarboxylation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Sex pheromone components of two species of arctiid moths, Estigmene acrea and Phragmatobia fuliginosa, were shown to be derived from linolenic acid. Female pupae were injected with radiolabeled malonic acid or an 18-, 20-, 21-, or 22-carbon triunsaturated fatty acid, and the pheromone components from emerged adults analyzed for radioactivity. The data support a biosynthetic pathway in which the 21-carbon pheromone component,(Z, Z)-3,6-cis-9,10-epoxyheneicosadiene, of these moths is produced by chain elongation of linolenic acid to docosatrienoic acid with subsequent reductive decarboxylation. The 18-carbon aldehyde components,(Z, Z)-9,12-octadecadienal and (Z, Z, Z)-9,12,15-octadecatrienal, of E. acrea are produced from linoeic and linolenic acids directly. No detectable amounts of intermediate 20-, 21-, or 22-carbon fatty acid precursors were found in the gland of E. acrea.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120203
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 20
    Electronic Resource
    Electronic Resource
    Sex pheromone biosynthesis in the housefly: Evidence for the regulation of the fatty acyl-CoA desaturation and elongation system by 20-hydroxyecdysone (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 173-186 
    Details
    ISSN: 0739-4462
    Keywords: stearoyl-CoA ; oleoyl-CoA ; erucoyl-CoA ; tetracosenoyl-CoA ; Musca domestica ; desaturase ; fatty acid chain elongation ; insect microsomes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The effects of age, sex, and 20-hydroxyecdysone treatments on fatty acyl-CoA desaturation and elongation, key reactions in sex pheromone biosynthesis in the housefly, Musca domestica, were investigated. Radio-HPLC analyses of the elongation products of [1-14C] 18: 1-CoA in the presence of malonyl-CoA and NADPH by microsomes prepared from 0-, 1-, 2-, 3-, and 4-day-old males and 0- and 1-day-old female houseflies showed that all even-numbered monounsaturated fatty acids up to 30 carbons were formed. Insects of these ages and sexes produce alkenes of 27 carbons and longer. When microsomes prepared from females 2, 3, and 4 days old (vitellogenic through postvitellogenic) were used, there was no elongation of [1-14C] 18: 1-CoA beyond the 24: 1 fatty acyl moiety. Similarly, neither [1-14C]22: 1-CoA nor [14, 15-3H]24: 1-CoA were efficiently elongated beyond the 24: 1-acyl moiety in mature females. Females 2-4 days old produce, as their major alkene, the sex pheromone component (Z)-9-tricosene (“muscalure,” Z9-23 Hy), and they use 24: 1-CoA as the fatty acyl precursor. The initial precursor for the long chain monoenoic fatty acids is oleic acid. Males treated with 20-hydroxyecdysone and 2-4-day-old females desaturated 18: O-CoA to 18: 1-CoA with 36-57% less efficiency than control males or previtellogenic females. These data demonstrate that 20-hydroxyecdysone is involved in the regulation of (Z)-9-tricosene production by altering both desaturation and elongation activities.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120305
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 21
    Electronic Resource
    Electronic Resource
    Production of antibodies to Manduca sexta cerebral neurosecretory cells (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 219-229 
    Details
    ISSN: 0739-4462
    Keywords: insect neuropeptide ; peptidergic neuron ; neurohormone ; prothoracicotropic hormone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Understanding the neuroendocrine regulation of insect development depends upon having antibody probes to the neurohormones involved, which are usually present at trace levels, making antibody generation difficult. This report describes a simple method for producing antibodies specific to cerebral neurosecretory cells (NSC) of the tobacco hornworm, Manduca sexta, and to the neurohormone(s) they produce. The method involves the isolation of only a few hundred NSC somata (∼ 0.3 μg of protein) that serve as the immunogen. The cerebral NSC used were the L-NSC III, the prothoracicotropes, that produce the prothoracicotropic hormone (PTTH), the principal neuroendocrine effector of insect molting and metamorphosis. A PTTH-containing extract of microsurgically isolated somata of the L-NSC III was injected intraperitoneally into a Balb/c mouse. The antiserum produced specifically immunostained the L-NSC III in wholemounts of brains from different developmental stages. This antiserum also contained antibodies directed against PTTH, as shown by its ability to inhibit the neurohormone's biological activity in an in vitro prothoracic gland bioassay. Such antiserum can be used to investigate the ontogeny and phylogeny of NSCs. With the hybridoma technique, monoclonal antibodies to individual NSC proteins (PTTH) could be obtained, circumventing the need to purify them for antibody production. This method should be applicable to comparable neurosecretory cell systems in other insect species.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120403
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 22
    Electronic Resource
    Electronic Resource
    Binding of octopamine to membranes from the white-eyed and wild-type housefly heads (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 57-71 
    Details
    ISSN: 0739-4462
    Keywords: cAMP ; receptor ; biogenic amine ; artifact ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In attempting to develop an octopamine (OA) receptor preparation with ready access to large amounts of tissue, we examined the binding of OA to membranes from the heads of white and red houseflies (Musca domestica L.). Binding was dependent on the presence of L-ascorbic acid in the medium. However, equilibrium was reached only over 24-36 h at 4°C and reversal of binding was also slow and incomplete. Scatchard analysis revealed at least two binding sites in the white-eyed housefly. A high-affinity site (Kd = 13.9 nM and Bmax = 3.9 pmol/mg protein) was present, but the majority of the binding had low affinity (Kd = 1130 nM and Bmax = 165 pmol/mg protein). Scatchard analysis revealed a low affinity in the red-eyed housefly (Kd = 240 nM and Bmax = 12 pmol/mg protein). Catecholamines were the best competitors for OA binding followed by phenolamines such as OA and synephrine. 5-Hydroxytryptamine was less effective. Phentolamine and mianserin, which are good antagonists of the ability of OA to stimulate adenylate cyclase in housefly head membranes, and formamidine and imidazolines, which are potent partial agonists of this adenylate cyclase, were poor competitors of OA binding. The slow kinetics, low affinity, large amount, and unconventional pharmacological profile of this binding is not congruent with it being a neuroreceptor. When the brain was dissected free from the head, less than 10% of the total specific binding of OA was found in the brain membrane fraction. This suggests that most of the binding of OA may be to cuticular sites that possibly are associated with the metabolism of catecholamines in cuticular synthesis. Thus, binding studies made with labeled catecholamines and phenolamines on insect tissues containing significant cuticular elements should be interpreted with caution.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100106
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 23
    Electronic Resource
    Electronic Resource
    Repetitive DNA interspersion patterns in diptera (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 105-113 
    Details
    ISSN: 0739-4462
    Keywords: mosquito ; genome ; satellite DNA ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A wide spectrum of repetitive DNA amounts and interspersion patterns is seen in mosquitoes and other dipterans. Using a simple and rapid technique, we show that these range from a minimal amount in five species of Anopheles through moderate amounts in Culex quinquefasciatus to large amounts in Aedes aegypti and Stomoxys calcitrans. Although Culex and Aedes are closely related and both have a considerable amount of interspersed repetitive DNA, the repetitive sequences are different between the two genera. These results and previously published information show that the amount of repetitive DNA and sequences involved have changed many times during the evolution of the Diptera.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100202
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 24
    Electronic Resource
    Electronic Resource
    Isolation of the vitellogenin-binding protein from locust ovaries (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 141-149 
    Details
    ISSN: 0739-4462
    Keywords: endocytosis ; binding protein ; vitellogenin ; locust ; affinity purification ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A rapid, efficient procedure for the isolation and purification of the vitellogenin binding protein from locust ovarian membranes is described. After solubilization with the nonionic detergent octyl-β-D-glucoside and removal of the detergent, the binding protein is subjected to affinity chromatography on vitellogenin coupled covalently to Affi-Gel 15. The binding protein is eluted with suramin and EDTA at low pH value. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis reveals a polypeptide with a molecular weight of 156,000 in the eluted fraction. By ligand blotting this polypeptide could be identified as the vitellogenin binding protein. It retains its high-affinity binding properties. The specific binding of vitellogenin increases from 4.8 μg (intact ovarian membranes) to 170.9 μg (affinity purified binding protein) per mg membrane protein, which corresponds to a purification factor of 35.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100205
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 25
    Electronic Resource
    Electronic Resource
    Endogenous and induced monooxygenase activity in gypsy moth larvae feeding on natural and artificial diets (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 47-56 
    Details
    ISSN: 0739-4462
    Keywords: Lymantria dispar ; Heliothis zea ; Estigmene acrea ; Diptera ; α-pinene ; pine ; oak ; MFO ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: NADPH oxidase activity was measured in third to sixth instar gypsy moth larvae fed oak or pine foliage. Activity levels ranged from 400 to 1,900 pmol NADPH oxidized/min/mg microsomal protein, but enzyme activity was not correlated with host plant ingested. Similarly, activity levels in larvae fed diets containing inducers, such as the terpenoid α-pinene or pentamethylbenzene, ranged from 700 to 1,500 pmol NADPH oxidized/min/mg protein, levels that were comparable to those measured for larvae fed control diets. O-demethylase activity in older instar gypsy moth larvae fed pine averaged 109 pmol p-nitrophenol/min/mg protein, and activity levels in those fed diet containing α-pinene ranged from 22 to 55 pmol/min/mg protein. Although statistically significant, these induced O-demethylase levels are well below those observed for Heliothis zea larvae. Our findings indicate that monooxygenases play a minor, if any, role in the ability of later instar gypsy moth larvae to develop successfully on pine foliage.
    Additional Material: 6 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100105
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 26
    Electronic Resource
    Electronic Resource
    Control of copulation-enhanced protein synthesis in the long hyaline gland of the male grasshopper, Melanoplus sanguinipes (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 13-19 
    Details
    ISSN: 0739-4462
    Keywords: accessory reproductive gland ; corpus allatum ; nervi corporis allati ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Control of copulation-enhanced protein synthesis in the accessory reproductive gland of the male grasshopper, Melanoplus sanguinipes, has been studied by measurement of in vivo incorporation of [35S]methionine into a juvenile hormone (JH)-regulated Mr 72,000 glycoprotein, long hyaline protein I (LHPI). In normal males, incorporation into LHPI was enhanced within 4 h of the commencement of mating and had increased even further when measured 24 h later. Short (15 min) copulations, in which small amounts of LHPI were discharged, stimulated incorporation into LHPI but brief genital contact did not. Neither severance of the nervi corporis allati nor allatectomy (CA-) on day 1 prevented copulation-enhancement of incorporation into LHPI. Decapitation after 15 min of copulation also failed to prevent copulation-enhanced incorporation into LHPI. This suggests that neither the CA nor the corpus cardiacum/brain complex is essential for the response. There was, however, a strong positive correlation between the amount of LHPI lost at copulation and the subsequent rate of incorporation into LHPI. These results suggest that control of copulation-enhanced incorporation of amino acids into LHPI is peripheral and linked to the extent of gland emptying.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110103
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 27
    Electronic Resource
    Electronic Resource
    Metabolism of dietary Δ8-sterols and 9β, 19-cyclopropyl sterols by Locusta migratoria (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 47-62 
    Details
    ISSN: 0739-4462
    Keywords: Triticum sativum ; fenpropimorph ; steryl esters ; ecdysteroids ; 24-methyl pollinastanol ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Adult female locusts were reared on wheat seedlings (experimental wheat) containing more than 97% of 9,10-cyclopropyl sterols and Δ8-sterols and less than 2% of Δ5-sterols. These insects showed a dramatic decrease in their cholesterol, cholestanol and Δ7-cholestanol content compared with control insects. These changes were more dramatic for steryl esters than for free sterols. Similar results were observed in eggs laid by the insects fed on experimental wheat. The decrease in Δ5-, Δ0- and Δ7-sterols in insects reared on experimental wheat was compensated by a marked accumulation of Δ8-sterols and 9β, 19-cyclopropyl sterols in the free sterol fraction and especially in the steryl ester fractions. The ecdysteroid content of eggs laid by experimental female insects was reduced by up to 80% compared with controls. These and other results suggest that the dietary 9β, 19-cyclopropyl sterols and Δ8-sterols cannot be used by Locusta in place of Δ5-sterols for ecdysteroid biosynthesis. To give support to this hypothesis, the experimental wheat was supplemented with various sterols before being presented to the insects immediately after the first egg laying. When cholesterol, sitosterol, or cholestanol were used as supplements, there was a complete recovery of the ecdysteroid titer in the eggs, a disappearance of 9β, 19-cyclopropyl sterols, and a restoration of the cholesterol content in both the animals and the eggs. Stigmasterol, stigmastanol, and ergosterol were much less efficient in reversing the effects of the experimental wheat. As expected, 9β, 19-cyclopropyl sterols were totally ineffective. These results are discussed in the light of our information on the role played by sterols in insect development and on the structural features required by the sterols to fulfill their role.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110106
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 28
    Electronic Resource
    Electronic Resource
    The effect of severing the dorsal vessel on egg production in Rhodnius prolixus (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 139-146 
    Details
    ISSN: 0739-4462
    Keywords: corpus allatum ; juvenile hormone ; neurohormone ; heart ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Severing the dorsal vessel (DV) behind the corpus allatum (CA), or in the anterior part of the abdomen of Rhodnius prolixus, greatly reduces egg production, an effect which is abolished by the topical application of juvenile hormone l (JH l). Severing the DV in the posterior abdomen does not result in a marked reduction of egg production, although severing the alary muscles in segments V and VI has a similar effect to severing the DV in the anterior abdomen. Reduced egg production caused by severing the DV on day 8 postemergence does not occur if the nerves connecting the CA to the brain are severed on day 1 post emergence. However, egg production is reduced if the DV is severed on day 1 post emergence and the connections between the brain and the CA severed on day 8, suggesting that inhibition of the CA caused by severance of the DV requires innervation from the brain. An isolated CA implanted into an animal decapitated immediately after feeding escapes from the inhibition imposed by severance of the DV. Conversely, the CA in an insect, the head of which has been decapitated just anterior to the CA, remains inhibited. This result suggests that the head posterior to the brain must be present to maintain inhibition. It is concluded that DV severance acts on the brain via some humoral influence to impose inhibition on the CA, and that an endocrine center in the head is required in order to maintain the inhibition.
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110302
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 29
    Electronic Resource
    Electronic Resource
    Juvenile hormone-like effects of a thiazolylurea on lepidopteran larvae (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 79-88 
    Details
    ISSN: 0739-4462
    Keywords: juvenile hormone analog ; insect development ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Heliothis virescens maintained on a diet containing 50 ppm of thiazolylurea (5-[[[2-thiazolylamino]amino]carbonyl]-1,3-benzenedicarboxylic acid dimethyl ester) showed symptoms of juvenile hormone overdose in the last larval instar. Increases in development time and weight, as well as larval color changes, were similar in animals fed thiazolylurea or topically treated with the juvenile hormone mimic methoprene. The juvenile hormone esterase titer profile in hemolymph of animals fed thiazolylurea was much broader than in controls, and peaked 2 days later than in controls; the premolt ecdysteroid peak in hemolymph of animals fed thiazolylurea appeared 2 days earlier than in controls. These events are characteristic of high hemolymph JH titers throughout the last larval instar.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120202
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 30
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120301
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 31
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120101
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 32
    Electronic Resource
    Electronic Resource
    Glutathione peroxidase activity in insects: A reassessment (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 31-49 
    Details
    ISSN: 0739-4462
    Keywords: antioxidant enzymes ; lipid perioxidation ; selenium metabolism ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In vertebrate species, cytotoxic H2O2 and other lipid or organic hydroperoxides (ROOH) formed in aerobic metabolism are removed by a selenoprotein, glutathione peroxidase (GPOX). The GPOX activity in most rat tissues ranges from 100 to 1,000 units (1 unit = 1 nmol NADPH oxidized·mg protein-1·min-1), except for muscles (20-30 units). In contrast, GPOX activities of two strains of the housefly (Musca domestica), cabbage looper (Trichoplusia ni), southern armyworm (Spodoptera eridania), and black swallowtail butterfly (Papilio polyxenes), were found to be in the range 2-12 units. Trivial GPOX activity was detected in the confused flour beetle (Tribolium confusum). In the earthworm (Lumbricus terrestris), banana slug (Ariolimax columbianus), and market squid (Loligo opalescens), the GPOX activity ranged from 1 to 5 units. Tissue selenium concentrations were about 500-1,000 ppb for adult M. domestica, 600 ppb in T. confusum, 32 ppb in T. ni, 17 ppb in S. eridania, and 31 ppb in P. polyxenes larvae. The form of selenium incorporated at such high levels in tissues of invertebrates such as M. domestica remains an unresolved issue. Peroxidase activity of non-selenium glutathione-S-transferase (GT) against ROOH may compensate for the low GPOX activity. Catalase (CAT) has high activity and wide subcellular distribution in insects. This may be an evolutionary adaptation to GT's inability to catalyze the reduction of H2O2. The GT's peroxidase and CAT activities were not assessed for other invertebrate species, and warrants an investigation due to their reported low GPOX levels.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120104
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 33
    Electronic Resource
    Electronic Resource
    Profiles of free and conjugated ecdysteroids and ecdysteroid acids during pupal-adult development of Manduca sexta (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 63-74 
    Details
    ISSN: 0739-4462
    Keywords: [14C]cholesterol ; HPLC ; ecdysteroid titers ; ecdysteroid metabolism ; epimerization ; hydroxylation ; oxidation ; epiecdysteroid acids ; epiecdysteroid phosphates ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The levels of individual free and conjugated ecdysteroids and ecdysteroid acids, labeled from [14C]cholesterol, in five different age groups of male Manduca sexta during pupal-adult development were determined by HPLC. Eight free ecdysteroids, eight ecdysteroid phosphates, and two ecdysteroid acids were identified. Newly ecdysed pupae contained predominantly 3-epiecdysteroids in each of the free, conjugated, and acidic ecdysteroid fractions. The titer of each ecdysteroid fraction rose sharply by day 4, and this was particularly noteworthy with respect to free ecdysone and 3-epi-20-hydroxyecdysonoic acid. This stage demonstrated high degrees of ecdysone biosynthesis, oxidative catabolism, and phosphorylation. As development proceeded to day 16, total ecdysteroid titer remained constant; a decreasing free ecdysteroid titer was accompanieid by increasing titers of both conjugates and acids resulting from the metabolic processes of hydroxylation, oxidation, epimerization, and phosphorylation. The predominant metabolites throughout development were 3-epi-20-hydroxyecdysonoic acid and the phosphate conjugates of 3-epi-20-hydroxyecdysone and 3-epi-20,26-dihydroxyecdysone. The ultimate inactivation of the ecdysteroids of M. sexta during pupal-adult development is possibly mediated by two pairs of metabolically-linked processes, one leading to a 3-epiecdysteroid acid, and the other to 3-epiecdysteroid phosphates.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120106
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 34
    Electronic Resource
    Electronic Resource
    Stimulated synthesis of the female-specific storage protein in male larvae of the silkworm Bombyx mori treated with juvenile hormone analog (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 99-109 
    Details
    ISSN: 0739-4462
    Keywords: dauer larvae ; methoprene ; allatectomy ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Application of methoprene to fourth (penultimate) instar larvae of the silkworm Bombyx mori induced the appearance of the feeding dauer larvae at the fifth (last) instar and prevented pupal metamorphosis. Methoprene also increased the protein concentrations of hemolymph last instar larvae by preventing sequestration of storage proteins by the fat body. Usually, the female-specific storage protein 1 (SP1)* disappears from the male hemolymph at the time of the last larval instar. However, exposure of male larvae to methoprene at the penultimate instar enhanced the accumulation of SP1 in the hemolymph. The SP1 accumulated in males did not differ in molecular weight and immunoreactivity from the SP1 produced in female larvae. Both sexes of fourth instar larvae allatectomized on day 1 instantly accumulated SP1 in the hemolymph, and methoprene application after allatectomy suppressed the hemolymph accumulation of the SP1. In contrast, if allatectomy was carried out at a later stage of the fourth larval instar, SP1 concentration in hemolymph of fifth instar larvae did not increase, suggesting the different juvenile hormone action for regulation of SP1 synthesis in the penultimate instar larvae of silkworms.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120204
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 35
    Electronic Resource
    Electronic Resource
    Characterization of quinone tautomerase activity in the hemolymph of Sarcophaga bullata larvae (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 157-172 
    Details
    ISSN: 0739-4462
    Keywords: insect immunity ; melanization ; prophenoloxidase activation ; quinone methide for mation ; quinone isomerase ; quinone detoxification ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The hemolymph of Sarcophaga bullata larvae was activated with either zymosan or proteolytic enzymes such as chymotrypsin or subtilisin and assayed for phenoloxidase activity by two different assays. While oxygen uptake studies readily attested to the wide specificty of activated phenoloxidase, visible spectral studies failed to confirm the accumulation of quinone products in the case of 4-alkyl substituted catechols such as N-acetyldopamine and N-β-alanyldopamine. Sepharose 6B column chromatography of the activated hemolymph resolved phenoloxidase activity into two fractions, designated as A and B. Peak A possessed typical o-diphenoloxidase (o-diphenol, oxygen oxidoreductase EC 1.10.3.1) activity, while peak B oxidized physiologically important catecholamine derivatives such as N-acetyldopamine, N-acetylnorepinephrine, and N-β-alanyldopamine into N-acetylnorepinephrine, N-acetylarterenone, and N-β-alanylnorepinephrine, respectively, and converted 3,4-dihydroxyphenylacetic acid, 3,4-dihydroxymandelic acid, and 3,4-dihydroxyphenylglycol into 3,4-dihydroxymandelic acid, 3,4-dihydroxybenzaldehyde, and 2-hydroxy-3′,4′-dihydroxyacetophenone, respectively. These transformations are consistent with the conversion of phenoloxidase-generated quinones to quinone methides and subsequent non-enzymatic transformations of quinone methides. Accordingly, Peak B contained both o-diphenoloxidase activity and quinone tautomerase activity. Sepharose 6B column chromatography of unactivated hemolymph resulted in the separation of quinone tautomerase from prophenoloxidase. The tautomerase rapidly converted both chemically made and mushroom tyrosinase-generated quinones to quinone methides. Thus the failure to observe the accumulation of quinones with N-acyl derivatives of dopamine and related compounds in the whole hemolymph is due to the rapid conversion of these long lived toxic quinones to short lived quinone methides. The latter, being unstable, undergo rapid non-enzymatic transformations to form side-chain-oxygenated products that are non-toxic. The possible roles of quinone isomerase and its reaction products - quinone methides - as essential components of sclerotization of cuticle and defense reaction of Sarcophaga bullata are discussed.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120304
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 36
    Electronic Resource
    Electronic Resource
    Metabolism of ecdysteroid by testes of the tobacco budworm, Heliothis virescens (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 83-92 
    Details
    ISSN: 0739-4462
    Keywords: lepidopteran ; biosynthesis ; steroid ; gonads ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Testes from late last stage larvae of the tobacco budworm, Heliothis virescens, were incubated with [3H]ecdysone and [3H]cholesterol. [3H]Ecdysone was converted to six other major ecdysteroids, identified by cochromatography in reverse-phase high-pressure liquid chromatography (RPHPLC); four of them were verified by normal-phase HPLC. A highly polar fraction, moderately polar ecdysteroids (20,26-dihydroxyecdysone, 3-epi-20-hydroxyecdysone, and 20-hydroxyecdysone) and low-polarity ecdysteroids, including 2-deoxyecdysone, were detected after incubation with [3H]ecdysone. Compounds that reacted positively to antibodies to progesterone and testosterone were detected in the low-polarity fractions. Testes were incubated in fractions corresponding to each of the major ecdysteroid peaks derived from [3H]ecdysone metabolism. Although most of the radioactive ecdysteroid fractions were further metabolized to high- and low-polarity endpoints, 88% of the [3H]20-hydroxyecdysone peak apparently remained unmetabolized. 20-Hydroxyecdysone may be the primary ecdysteroid product of testes of H. virescens. [3H]Cholesterol was not metabolized to any appreciable extent.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100108
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 37
    Electronic Resource
    Electronic Resource
    Announcements (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 175-175 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100208
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 38
    Electronic Resource
    Electronic Resource
    Persistence and effects of α-methyl-substituted amino acids on 5-hydroxytryptamine and dopamine concentrations in cockroach (Periplaneta americana) nervous tissue (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 163-174 
    Details
    ISSN: 0739-4462
    Keywords: α-methyltryptophan ; α-methyltyrosine ; α-methyldihydroxyphenylalanine ; 5-hydroxytryptamine ; dopamine, insect ; cockroach (Periplaneta americana) ; nervous tissue ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The α-methylated derivatives of tryptophan, tyrosine, and dihydroxyphenylalanine were injected into cockroaches (Periplaneta americana). The levels of these compounds and those of dopamine, 5-hydroxytryptamine, tyrosine, and tryptophan in the nervous tissue, hemolymph, and fat body were measured at various times after drug administration. Levels of 5-hydroxytryptamine and tryptophan in the nervous tissue are significantly reduced by α-methyltryptophan administration. Concentrations of dopamine in nervous tissue are reduced by α-methyltyrosine administration. This effect also persists for several weeks, and α-methyltyrosine is observed in the nervous tissue 3 weeks after injection. Levels of dopamine and 5-hydroxytryptamine in the nervous tissue are unaffected by α-methyldihydroxyphenylalanine, and this compound is less persistent in nervous tissue than α-methyltyrosine or α-methyltryptophan demonstrates that these compounds can be absorbed and affect amine levels in the nervous tissue when included in the diet. Inhibition of tryptophan hydroxylation by crude enzyme preparations of cockroach nervous tissue was demonstrated with both α-methyltryptophan and α-methyltyrosine, with α-methyltryptophan being the more effective inhibitor. Aromatic amino acid decarboxylase activity toward dihydroxyphenylalanine in crude enzyme preparations of cockroach nervous tissue was strongly inhibited by α-methyldihydroxyphenylalanine and monofluoromethyldihydroxyphenylalanine, slightly inhibited by α-methyltyrosine and unaffected by α-methyltryptophan at concentrations up to 10-3 M. The results indicate that α-methyltyrosine and α-methyltryptophan, but not α-methyldihydroxyphenylalanine, can selectively alter amine concentrations in insect nervous tissue and that insects are only poorly able to metabolize or excrete these compounds. The selective and long-lasting depletion of dopamine or 5-hydroxytryptamine by some of these compounds suggest that they may be useful in behavioral studies designed to elucidate the roles of these amines in insects.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100207
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 39
    Electronic Resource
    Electronic Resource
    Identification of a pheromone blend attractive to Manduca sexta (L.) males in a wind tunnel (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 255-271 
    Details
    ISSN: 0739-4462
    Keywords: insect behavior ; aldehydes ; 10 ; 12 ; 14-hexadecatrienal ; tobacco hornworm ; Sphingidae ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Analyses of solvent rinses of the external surfaces of pheromone glands excised from calling female tobacco hornworm moths, Manduca sexta (L.), revealed the presence of the following compounds: (Z)-9-hexadecenal, (Z)-11-hexadecenal, (E)-11-hexadecenal, hexadecanal, (E,Z)-10,12-hexadecadienal, (E,E)-10,12-hexadecadienal, (E,E,Z)-10,12,14-hexadecatrienal, (E,E,E,)-10,12,14-hexadecatrienal, (Z)-11-octadecenal, (Z)-13-octadecenal, octadecanal, and (Z,Z)-11,13-octadecadienal. The two trienals were identified by mass and PMR spectral analyses and by ozonolyses, and their structures were confirmed by synthesis. In a wind tunnel male tobacco hornworm moths exhibit the same behaviors in response to a synthetic blend of all of the components, the gland rinse, or a calling female. Both (E,Z)-10,12-hexadecadienal and (E,E,Z)-10,12,14-hexadecatrienal are required to stimulate males to complete the characteristic behavioral sequence: anemotaxis, approaching and touching the pheromone source, and bending their abdomens in apparent copulatory attempts. The other components of the blend may play more subtle roles.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100402
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 40
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100101
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 41
    Electronic Resource
    Electronic Resource
    On the oxidation of 3,4-dihydroxyphenethyl alcohol and 3,4-dihydroxyphenyl glycol by cuticular enzyme(s) from Sarcophaga bullata (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 13-27 
    Details
    ISSN: 0739-4462
    Keywords: insect cuticle ; catecholamine metabolism ; quinone methide sclerotization ; quinone tanning ; phenoloxidase ; quinone tautomerase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The catabolic fate of 3,4-dihydroxyphenethyl alcohol (DHPA) and 3,4-dihydroxyphenylethyl glycol (DHPG) in insect cuticle was determined for the first time using cuticular enzyme(s) from Sarcophaga bullata and compared with mushroom tyrosinase-medicated oxidation. Mushroom tyrosinase converted both DHPA and DHPG to their corresponding quinone derivatives, while cuticular enzyme(s) partly converted DHPA to DHPG. Cuticular enzyme(s)-mediated oxidation of DHPA also accompanied the covalent binding of DHPA to the cuticle. Cuticle-DHPA adducts, upon pronase digestion, released peptides that had bound catechols. 3,4-Dihydroxyphenyl-acetaldehyde, the expected product of side chain desaturation of DHPA, was not formed at all. The presence of N-acetylcysteine, a quinone trap, in the reaction mixture containing DHPA and cuticle resulted in the generation of DHPA-quinone-N-acetylcysteine adduct and total inhibition of DHPG formation. The insect enzyme(s) converted DHPG to its quinone at high substrate concentration and to 2-hydroxy-3′,4′-dihydroxyacetophenone at low concentration. They converted exogenously added DHPA-quinone to DHPG, but acted sluggishly on DHPG-quinone. These results are consistent with the enzymatic transformations of phenoloxidase-generated quinones to quinone methides and subsequent nonenzymatic transformation of the latter to the observed products. Thus, quinone methide formation in insect cuticle seems to be caused by the combined action of two enzymes, phenoloxidase and quinone tautomerase, rather than the action of quinone methide-generating phenoloxidase (Sugumaran: Arch Insect Biochem Physiol 8, 73-88, 1988). It is proposed that DHPA and DHPG in combination can be used effectively to examine the participation of (1) quinone, (2) quinone methide, and (3) dehydro derivative intermediates in the metabolism of 4-alkylcatechols for cuticular sclerotization.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100103
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 42
    Electronic Resource
    Electronic Resource
    Apolar conjugates of ecdysteroids are not used as a storage form of molting hormone in the argasid tick Ornithodoros moubata (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. I 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Fifth (last) instar nymphs of th e tick Ornithodoros moubata convert ingested 20-hydroxyecdysone (20E) to apolar conjugates AP2, which are then converted to th e more polar conjugates API. Only small quantities of free hormone were transferred to th e hemolymph and the carcass within t h e first 2 days after the blood meal. The proportion of radiolabel in these two compartments was highest at the time of the endogenous ecdysteroid peak; however, no traces of free [3H]20E were detected. The conversion probably occurs principally in the intestinal cells. Eleven days after ingestion, 84% of the radiolabel is located in the digestive tract, mainly in the form of API conjugates.API obtained in second instar nymphs fed with [3H]ecdysone ([3H]E) remain stable throughout the following nymphal instars. The ecdysteroid moiety of APT remained unchanged. The hydrolysis, although not complete, always yielded a peak comigrating with the reference E but never 20E or any other clearly distinct peaks that may have corresponded to metabolites of 20E. Less label per individual was present in adults, but its nature remained the same, viz., API mainly located in the digestive tract. In females, 2.5% of the label was transferred to the progeny during the first ovipositional cycle.Apolar products (mainly AP2) that accumulated in eggs of females injected with [3H]E or [3H]20E during vitellogenesis remained unchanged during the whole embryonic development. During the molting cycle of larvae, there was only a slight conversion of AP2 to API, but esterase hydrolysis of these products released the same percentages of E and 20E as in the freshly laid eggs.We conclude that in this tick species apolar conjugates of ecdysteroids are inactivation metabolites that are not reutilized during the development of the animal. These metabolites are mainly retained in the tick, probably because of its peculiar blocked midgut. Several studies have shown that in other arthropod species (ticks, spiders, and insects), these apolar metabolites are excreted in the feces.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100308
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 43
    Electronic Resource
    Electronic Resource
    Knockdown resistance to dichlorodiphenyl-trichloroethane and pyrethroid insecticides in the napts mutant of Drosophila melanogaster is correlated with reduced neuronal sensitivity (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 293-302 
    Details
    ISSN: 0739-4462
    Keywords: deltamethrin ; fenfluthrin ; sodium channel ; electrophysiology ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Resistance to pyrethroid insecticides and dichlorodiphenyltrichloroethane (DDT) was investigated in the napts (no action potential, temperature sensitive) mutant of Drosophila melanogaster. In surface contact bioassays, the napts strain showed threefold resistance to deltamethrin at the LC50 level when compared to susceptible Canton-S flies. Cross-resistance was also observed to DDT and the pyrethroids NRDC 157 [3-phenoxybenzyl [1R,cis]-3-(2,2-dibromovinyl)-2,2-dimethylcyclopropanecarboxylate], fenfluthrin, and MTI-800 [1-(3-phenoxy-4-fluorophenyl)-4-(4-ethoxyphenyl)-4-methylpentane]. The onset of intoxication by pyrethroids in napts flies was markedly delayed, a finding that is consistent with the existence of a resistance mechanism involving reduced neuronal sensitivity. Resistance at the level of the nerve was confirmed by electrophysiological recordings of spontaneous and evoked activity in the dorsolongitudinal flight muscles of poisoned flies. Preparations from napts insects treated with fenfluthrin displayed longer latencies to the appearance of spontaneous activity and also an absence or reduction in burst discharges compared to equivalent preparations from susceptible individuals. These results are discussed in light of competing hypotheses concerning the mechanism underlying knockdown resistance and reduced nerve sensitivity in insects.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100405
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 44
    Electronic Resource
    Electronic Resource
    Changes in the titer of the female-predominant storage protein (81K) during larval and pupal development of the waxmoth, galleria mellonella (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 333-348 
    Details
    ISSN: 0739-4462
    Keywords: serum proteins ; immunoelectrophoresis ; development ; insect ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The levels of an 81K storage protein in the waxmoth, Galleria mellonella, were monitored during the course of development using rocket immunoelectrophoresis. During the fifth and sixth larval stadia, 81K protein levels increased during feeding and growth but sharply declined at each larval molt. During the fifth and sixth stadia hemolymph levels of the 81K protein increased to about 1 and 2.5 mg/ml, respectively, with no discernible differences between levels in males and females. Neither the fat body nor the remainder of the carcass contained the 81K protein, indicating that the accumulation of this protein during the intermolt period was exclusively in the hemolymph and redistribution of the 81K protein into other tissues does not occur at the final two larval molts. During the seventh (final) larval stadium the absolute quantities of the 81K protein increased from 23 μg per insect to over 1,600 μg in females and to 300 μg in males. The hemolymph concentration of the 81K protein reached 28 mg/ml in females and 6 mg/ml in males with only low levels found in the remaining tissues. Shortly after pupal apolysis, marked by eyespot retraction, the fat body in both sexes rapidly and quantitatively sequestered the 81K protein from the hemolymph. The 81K protein in the hemolymph of both males and females rapidly dropped to nearly zero concentration by pupation. The 81K storage protein remained localized in the fat body cells after uptake occurred, even though the fat body cells disaggregate and reaggregate during metamorphosis. During pharate adult development the 81K storage protein disappeared from the fat body without entering the hemolymph. At adult eclosion 81K was virtually absent from the tissues of both males and females.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100408
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 45
    Electronic Resource
    Electronic Resource
    Meeting announcements (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 63-63 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110107
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 46
    Electronic Resource
    Electronic Resource
    Xenobiotic absorption and binding by proteins in hemolymph of the weevil Diaprepes abbreviatus (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 65-78 
    Details
    ISSN: 0739-4462
    Keywords: insect hemolymph proteins ; fluorescence spectroscopy ; native electrophoresis ; root weevils ; Coleoptera ; Curculionidae ; citrus ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A synthetic coumarin, 7-amino-3-phenyl coumarin (coumarin-10), was used to study the uptake of ingested xenobiotics into hemolymph. Larvae were forcefed coumarin-10 in peanut oil, and hemolymph was extracted and analyzed by fluorescence spectroscopy. Coumarin-10 entered hemolymph within 5 min, reaching a steady state of concentration within 1 h. Assayed 2 h after feeding, hemolymph titers of 1-5 ng/μl were proportional to log dose between 10 and 100 ng/mg body weight; hemolymph did not reach saturation. Fluorescence spectra of hemolymph in saline revealed that energy was readily transferred from hydrophobic residues of hemolymph proteins to coumarin-10. Ultracentrifugal density gradients revealed that 94% of absorbed coumarin-10 was bound to sedimenting proteins while 6% bound to lipophorin. Native polyacrylamide gel electrophoresis (N-PAGE) on minigels identified two major proteins responsible for binding. Though readily separated by native electrophoresis, these proteins were not fully separable by HPLC using a wide variety of columns. Gel permeation-HPLC of the sedimenting proteins from hemolymph revealed a single major peak of 480,000 Mr. When upper and lower electrophoretic bands were isolated by preparative N-PAGE, the upper band (band I) yielded subunits of 75,000 and 71,000 Mr, while the lower band (band II) yielded only one size subunit of 75,000 Mr on denaturing (SDS) PAGE. The fluorescent products bound by sedimenting proteins were identified by thin-layer chromatography and scanning fluorescence densitometry as coumarin-10 (80% of total) and a polar metabolite (20%). In addition, lipophorin-containing fractions contained an apolar metabolite (3% of total fluorescence). In vitro binding studies utilizing fluorescent energy transfer demonstrated saturation binding with a KD of 1.5 μM.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110202
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 47
    Electronic Resource
    Electronic Resource
    Further studies on the mechanism of oxidation of N-acetyldopamine by the cuticular enzymes from Sarcophaga bullata and other insects (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 109-125 
    Details
    ISSN: 0739-4462
    Keywords: quinone tanning ; quinone methide sclerotization ; phenoloxidase ; quinone:quinone tautomerase ; desaturase ; 1,2-dehydro-N-acetyldopamine ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In accordance with our earlier results, quinone methide formation was confirmed to be the major pathway for the oxidation of N-acetyldopamine (NADA) by cuticle-bound enzymes from Sarcophaga bullata larvae. In addition, with the use of a newly developed HPLC separation condition and cuticle prepared by gentle procedures, it could be demonstrated that 1, 2-dehydro-NADA and its dimeric oxidation products are also generated in the reaction mixture containing a high concentration of NADA albeit at a much lower amount than the NADA quinone methide water adduct, viz., N-acetylnorepinephrine (NANE). By using different buffers, it was also possible to establish the accumulation of NADA quinone in reaction mixtures containing NADA and cuticle. That the 1,2-dehydro-NADA formation is due to the action of a NADA desaturase system was established by pH and temperature studies and by differential inhibition of NANE production. Of the various cuticle examined, adult cuticle of Locusta migratoria, presclerotized cuticle of Periplaneta americana, and white puparial cases of Drosophila melanogaster exhibited more NADA desaturase activity than NANE generating activity, while the reverse was observed with the larval cuticle of Tenebrio molitor and pharate pupal cuticle of Manduca sexta. These studies indicate that both NADA quinone methide and 1, 2-dehydro NADA are formed during enzymatic activation of NADA in insect cuticle. Based on these results, a unified mechanism for β-sclerotization involving quinone methides as the reactive species is presented.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110205
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 48
    Electronic Resource
    Electronic Resource
    Binding of juvenile hormone III to lipophorin from the american cockroach Periplaneta americana (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 159-172 
    Details
    ISSN: 0739-4462
    Keywords: JH-binding protein ; hemolymph proteins ; apolipophorin I ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Whole hemolymph from the American cockroach, Periplaneta americana, efficiently binds juvenile hormone (JH) III and to a lesser extent JH-I and 10, 11-epoxyfarnesyl diazoacetate (EFDA). The dissociation constants for racemic JH-III and EFDA are 30 ± 2 nM and 1.0 μM, respectively. Isolated lipophorin also binds [3H]JH-III and to a lesser extent JH-I. Other proteins from the hemolymph do not bind JH-III. Binding of JH-III to lipophorin is enantioselective. The dissociation constant, measured with a 92% 10R and 8% 10S mixture, is 21 ± 2 nM. Each lipophorin molecule contains one specific binding site for JH-III. It is concluded that lipophorin is the JH-III-specific transport protein in the hemolymph of the American cockroach. By a combination of photoaffinity labelling and gradient electrophoresis with sodium dodecyl sulphate on polyacrylamide gel, we showed that the JH-III-specific binding site is probably located on apolipophorin I.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110304
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 49
    Electronic Resource
    Electronic Resource
    Juvenile hormone biosynthesis and oocyte development in adult female Blattella germanica: Effects of grouping and mating (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 189-200 
    Details
    ISSN: 0739-4462
    Keywords: brain disinhibition ; receptivity ; ootheca ; cockroach ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The roles of grouping and mating in modulating the activity of the corpora allata (CA) in adult female cockroaches were investigated using the in vitro radiochemical assay of juvenile hormone (JH) biosynthesis. Isolated virgin females have longer, asynchronous cycles of CA activity and oocyte maturation than do isolated females mated on day 8. Three factors were identified as the major contributors to this difference: (1) an experimental artifact of selection for sexually receptive females, (2) a positive effect of grouping on JH synthesis and oocyte maturation, and (3) a positive effect of copulation on oviposition and retention of the ootheca. Mated females constitute a subpopulation of receptive females that differ significantly from other females by having higher rates of JH synthesis prior to mating. The relative importance of such selection is substantial when the rate of mating is low, as in experiments with isolated females that are exposed to males for a short period of time. Long-term exposure of females to males introduces a grouping effect, which obscures any additional effect of mating on CA activity and oocyte development. However, mating influences ootheca formation and its retention. The effect of grouping can be mimicked in isolated females by transection of the nerves connecting the CA-corpora cardiaca complex to the brain, suggesting that in this insect isolation causes brain inhibition of the CA, and grouping provides disinhibitory stimuli that release the CA from brain inhibition.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110306
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 50
    Electronic Resource
    Electronic Resource
    Nonvitellogenic female protein in Musca domestica (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 245-255 
    Details
    ISSN: 0739-4462
    Keywords: housefly ; hemolymph proteins ; vitellogenesis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: During vitellogenesis in Musca domestica, a major hemolymph protein, in addition to vitellogenin, appears preferentially in females. This protein is synthesized by the adult fat bodies, secreted into the hemolymph, and is not taken up by the ovaries during vitellogenesis. We have designated this protein nonvitellogenic female protein (NVFP). It is composed of only one type of polypeptide (Mr=70,000) and occurs in two different forms. Synthesis of NVFP is induced by a protein diet, attaining maximum concentrations in females at the middle of the gonotrophic cycle. In males its maximum concentration never surpasses 10% of the concentration in females. The quantitative variation of the NVFP is cyclic and coincident with the gonotrophic cycles of Musca domestica.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110405
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 51
    Electronic Resource
    Electronic Resource
    Action of antioxidant enzymes and cytochrome P-450 monooxygenases in the cabbage looper in response to plant phototoxins (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 151-162 
    Details
    ISSN: 0739-4462
    Keywords: catalase ; detoxification ; glutathione peroxidase ; glutathione reductase ; induction ; superoxide dismutase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Effects of two biosynthetically distinct plant phototoxins - xanthototoxin, a furanocoumarin, and harmine, a β-carboline alkaloid, which are known to produce toxic oxygen species - on the food utilization efficiencies and enzymatic detoxification systems of the polyphagous cabbage looper. Trichoplusia ni (Lepidoptera: Noctuidae), were studied. Newly molted fifth-instar larvae were allowed 36 h to ingest diets containing these two phototoxins at 0.15% wet weight in the presence of near ultraviolet (UVA). The growth and development of the larvae, as well as the corresponding activities of the antioxidant enzymes superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPOX), and glutathione reductase (GR) and the detoxification enzyme cytochrome P-450, were measured. Xanthotoxin reduced rates of relative growth and consumption and efficiencies of conversion of ingested and digested food to biomass. Harmine reduced rates of growth and consumption without affecting efficiencies of conversion. Specific activities of SOD, CAT, GPOX, and GR of whole-body homogenates in the absence of compounds were 0.88 units, 153μmol H2O2 decomposed·mg protein-1·min - 1, 38.3 nmol NADPH oxidized·mg protein-1·min-1, and 0.56 nmol NADPH oxidized·mg protein-1·min-1, respectively. SOD activity was induced 2.9-fold and 3.8-fold by dietary xanthotoxin and harmine, respectively. CAT and GPOX activities were induced 1.2-fold by harmine only, and GR activity was not changed by either chemical. The P-450 activity toward xanthotoxin in the microsomal fraction of midguts was low (0.15 nmol xanthotoxin metabolized·mg protein-1·min-1) and was not induced by xanthotoxin ingestion. These studies indicate that P-450 and antioxidant enzyme systems may be independent but consequential, the induction of antioxidant enzymes by phototoxins occurring when low P-450 activity toward the phototoxin permits the accumulation of oxidative stress from unmetabolized phototoxin, which in turn induces antioxidant enzymes.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100206
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 52
    Electronic Resource
    Electronic Resource
    Synthesis and nuclear magnetic resonance study of 3-dehydroecdysteroids (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 199-213 
    Details
    ISSN: 0739-4462
    Keywords: ecdysteroids ; proton NMR ; carbon NMR ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Several 3-dehydro- (or 3-oxo-) ecdysteroids have been prepared by enzymatic and/or chemical means. Methods for their purification using various high-performance liquid chromatography systems are described. Proton and carbon nuclear magnetic resonance analyses show that 3-dehydroecdysteroids when dissolved in water or methanol (but not in chloroform) present a temperature-dependent equilibrium between two forms. The possible structure of these two forms is discussed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100304
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 53
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100401
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 54
    Electronic Resource
    Electronic Resource
    Pheromone receptor cells in the male moth Manduca sexta (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 273-279 
    Details
    ISSN: 0739-4462
    Keywords: olfaction ; sex pheromone ; electrophysiology ; antenna ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Three types of pheromone receptor cells have been identified by electrophysiological recording from single antennal sensilla trichodea of the male sphinx moth Manduca sexta. These cells responded best to the pheromone components (E,Z)-10,12-hexadecadienal (type A receptor cell), (E,E,Z)-10,12,14-hexadecatrienal (type B), and (E,E,E)-10,12,14-hexadecatrienal (type C). Cell type B also responded to (E,Z)-11,13-pentadecadienal, which has been used experimentally as a pheromone substitute. In recordings from 20 trichoid hairs, 17 were found to be innervated by one cell of type A and one of type B; 3 trichoid hairs had cell types A and C.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100403
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 55
    Electronic Resource
    Electronic Resource
    Degradation of juvenile hormone and methylation of juvenile hormone acid by corpora cardiaca-corpora allata of the cockroach, Nauphoeta cinerea: II. Physiological aspects (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 317-331 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In vitellogenic females of Nauphoeta cinerea, injected (10R)-juvenile hormone (JH) III was degraded more rapidly than racemic JH III: we measured a half-life of 21 min (with or without coinjection of lipophorin) for the former and 24 min (with coinjection of lipophorin) and 43 min (without coinjection of lipophorin) for the latter. One to two hours after injection, JH III acid was the major metabolite observed; in addition, several highly polar products were found. The half-life of injected racemic JH III acid was 19 min with coinjection of lipophorin and 4 min without. The JH III acid titer in hemolymph was low (around 5-10 pmol/ml) in last instar larvae and previtellogenic and pregnant females and reached higher values (40-100 pmol/ml) in vitellogenic and ovulating females. Racemic JH III acid could be methylated in vitro to JH III by corpora cardiaca-corpora allata (CC-CA) from penultimate instar larvae and females at stages between adult ecdysis and ovulation and at the very end of pregnancy, but not by CC-CA from last instar larvae and adult females at earlier stages of pregnancy. This indicates that CC-CA are capable of methylating JH III acid only at stages when JH III is detectable in the hemolymph. In double-labelling experiments with CC-CA from vitellogenic females and L-[14C]methionine and [3H]JH III acid as precursors, we observed that only a small proportion (1-8%) of total biosynthesized JH III was derived from JH III acid when the latter was present at physiological concentration. This suggests that in vivo recycling of JH III acid by CC-CA plays only a minor role in the regulation of the titer of JH III and JH III acid.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100407
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 56
    Electronic Resource
    Electronic Resource
    Intestinal amino acid absorption in tobacco hornworm larvae is stimulated by potassium and sodium but not rubidium or lithium (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 21-28 
    Details
    ISSN: 0739-4462
    Keywords: phenylalanine-alkali metal ion cotransport ; brush border membrane vesicles ; Manduca sexta ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We used rapid filtration assays to determine the ion selectivity of ion gradientdriven phenylalanine uptake by brush border membrane vesicles prepared from the larval midgut of the tobacco hornworm (Manduca sexta). Phenylalanine uptake by these vesicles is stimulated by both potassium and sodium. Phenylalanine uptake by larval M. sexta midgut brush border membrane vesicles is voltage sensitive and shows little selectivity for potassium over sodium. However, phenylalanine uptake by these vesicles is stimulated by neither rubidium nor lithium.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110104
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 57
    Electronic Resource
    Electronic Resource
    Effects of potential inhibitors on N-acetylation of octopamine by tissue extracts from malpighian tubules and cerebral ganglia of Periplaneta americana L (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 29-45 
    Details
    ISSN: 0739-4462
    Keywords: N-acetyltransferase ; dopamine ; 5-hydroxytryptamine ; formamidines ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: N-acetyltransferase activity in extracts of Malpighian tubules and cerebral ganglia from Periplaneta americana L. was monitored using high performance liquid chromatography with coulometric electrochemical detection. Several potential inhibitors were tested against the tissue preparations, and the results indicate distinct differences in the nature of the enzyme derived from the two sources. The Malpighian tubule and cerebral ganglia extracts were sensitive to sulfhydryl inhibition and divalent cations, and both preparations also showed end-product inhibition with coenzyme A. Juglone, an inhibitor of choline acetyltransferase, inhibits N-acetyltransferase activity from both tissues; however, separate studies with choline indicate that the N-acetylation observed in this study is not due to choline acetyltransferase. A number of phenyl, phenol, catechol and indole derivatives were tested and the results indicate that the presence of a 4-hydroxyl group on the phenol ring enhances the capacity of phenol and catechol derivatives to inhibit N-acetyltransferase. Demethylchlordimeform inhibits the production of N-acetyl-p-Octopamine by Malpighian tubule preparations and intact tissues whereas other formamidines, BTS-27271 and amitraz, inhibit N-acetyl-p-Octopamine production only in intact tissues.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110105
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 58
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110301
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 59
    Electronic Resource
    Electronic Resource
    Changes in the hemolymph of the stable fly, Stomoxys calcitrans, after a blood meal (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 147-158 
    Details
    ISSN: 0739-4462
    Keywords: hemolymph volume ; osmotic pressure ; cations ; anions ; ion chromatography ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The stable fly hemolymph was analyzed after a blood meal. The hemolymph volume increased to approximately three times the pre-feeding level 3-6 h after a blood meal and gradually returned to normal 18 h after the blood meal. The osmotic pressure decreased approximately 10% following a blood meal and gradually returned to normal with a pattern that was a mirror-image of that of the hemolymph volume. Concentrations of cations and anions are not directly affected by the ingested blood, indicating a possible selective excretory mechanism.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110303
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 60
    Electronic Resource
    Electronic Resource
    Erratum (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 201-201 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110307
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 61
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110401
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 62
    Electronic Resource
    Electronic Resource
    Ecdysone oxidase and 3-oxoecdysteroid reductases in Manduca sexta midgut: Kinetic parameters (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 201-218 
    Details
    ISSN: 0739-4462
    Keywords: 3-epimerization ; 3-dehydroecdysone ; 3-epiecdysone ; 3α-hydroxyecdysteroids ; 3β-hydroxyecdysteroids ; NADH ; NADPH ; molting hormone inactivation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Ecdysone and 20-hydroxyecdysone are converted to their 3-epimers by enzymes in the midgut cytosol of Manduca sexta larvae. A partially purified cytosol preparation has been used to analyze the nature of and the interaction between these enzymes. The cytosol was shown to contain ecdysone oxidase, one or more 3-oxoecdysteroid 3α-reductase(s), and one or more 3-oxoecdysteroid 3β-reductase(s). The reductases reacted at different velocities with NADH and NADPH. With NADH, 3α-reduction was the major reaction; with NADPH, 3β-reduction was the major reaction. The apparent kinetic parameters for the enzymes support the assumed two-step mechanism for the 3-epimerization with a 3-oxoecdysteroid as intermediate.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120402
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 63
    Electronic Resource
    Electronic Resource
    High-affinity uptake of [3H]serotonin in cultured neurones of the cockroach Periplaneta americana (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 253-266 
    Details
    ISSN: 0739-4462
    Keywords: avermectin ; formamidine ; ion-channel blocker ; neurotoxicant ; pesticide ; pyrethroid ; sodium gradient ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Cultured central neurons from the American cockroach, Periplaneta americana, have been used to investigate the uptake of [3H]serotonin. The neurones accumulate [3H]serotonin from the extracellular medium by both a high-and a low-affinity system. The activity of the high-affinity mechanism is decreased by low temperature and metabolic poisons, and is dependent on sodium and chloride ions. Both depolarising levels of external potassium ions and veratridine decrease the high-affinity uptake system, suggesting it is influenced by the transmembrane potential. The pyrethroid insecticides, deltamethrin and permethrin, enhance the inhibitory effect of veratridine. Pyrethroid enhancement is completely blocked by tetrodotoxin, and neither pyrethroid affects the uptake system in the absence of veratridine. Avermectin B1A is a powerful inhibitor of the high-affinity uptake system, and its effect is blocked by picrotoxin. High-affinity uptake of [3H]serotonin is inhibited by imipramine and amitriptyline; desipramine has no significant effect on this uptake. The activity of the high-affinity system is also reduced by 8-hydroxy-dipropylaminotetralin, α-methyl-serotonin, and 1-(3-chlorophenyl)piperazine. Dopamine, noradrenaline, octopamine, and the formamidine insecticides, chlordimeform and demethylchlordimerform, are moderate inhibitors of the high-affinity uptake system. The formamidine effect is not blocked by tetrodotoxin or picrotoxin.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120405
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 64
    Electronic Resource
    Electronic Resource
    Neither barium nor calcium prevents the inhibition by Bacillus thuringiensis δ-endotoxin of sodium- or potassium gradient-dependent amino acid accumulation by tobacco hornworm midgut brush border membrane vesicles (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 267-277 
    Details
    ISSN: 0739-4462
    Keywords: phenylalanine ; cotransport ; Manduca sexta ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Rapid filtration assays were used to determine the effects of barium, calcium and an insecticidal δ-endotoxin from Bacillus thuringiensis on sodium and potassium ion gradient dependent phenylalanine accumulation by brush border membrane vescles from the larval midgut of the tobacco hornworm (Manduca sexta). Neither barium nor calcium had a significant effect on sodium ion gradient dependent phenylalanine accumulation by the membrane vesicles. Both barium and calcium inhibited potassium ion gradient dependent phenylalanine accumulation by the membrane vesicles. B. thuringiensis δ-endotoxin inhibited both sodium and potassium ion gradient dependent phenylalanine accumulation by the vesicles. Inhibition of both sodium and potassium ion gradient dependent phenylalanine accumulation increased similarly with increasing δ-endotoxin inhibition of either sodium or potassium dependent phenylalanine accumulation by the vesicles.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120406
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 65
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120401
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 66
    Electronic Resource
    Electronic Resource
    Regional differentiation of fat bodies in larvae of the indianmeal moth, Plodia interpunctella (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 187-199 
    Details
    ISSN: 0739-4462
    Keywords: storage proteins ; lepidopteran ; mitochondria ; metamorphosis ; ultrastructure ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Larvae of the Indianmeal moth, Plodia interpunctella, contain two morphologically distinct fat bodies. Tan-colored, highly tracheated fat body located posteriorly in the abdomen was the predominant fat body tissue during the early larval instars. White, sheet fat body located more anteriorly became the predominant type during the fifth (last) larval instar and eventually occupied most of the space of the hemocoel. Ultrastructural morphology of tan fat body showed the tissue to be composed of cells containing numerous, large, spherical mitochondria, with only few lipid, glycogen, or protein storage structures. In contrast, white fat body was composed of cells that in later larval stages had organelles typical of storage functions. Both fat bodies produced storage proteins during the late fifth instar, whereas only white fat body accumulated the storage proteins. Tan fat body dispersed and apparently autolyzed in pharate pupae, whereas the white fat body metamorphosed and persisted into the adult stage. These observations indicate that fat body of the Indianmeal moth is functionally and morphologically differentiated along the anterior-posterior axis into two regional subgroups of cells.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120306
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 67
    Electronic Resource
    Electronic Resource
    Two hypolipidemic agents, cholestyramine and niacin, affect the development and lipid content of Heliothis zea (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 231-252 
    Details
    ISSN: 0739-4462
    Keywords: sterols ; acylglycerides ; glycerol ; hemolymph ; corn earworm ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Two vertebrate hypolipidemic agents, cholestyramine and niacin, affected the growth and development of Heliothis zea as well as the quantity of acylglyceride or sterol present in the larva. As the concentration of cholestyramine in the diet increased to 6.0%: the number of larval molts increased from 5 or 6 to as many as 7 or 8, the time required for the onset of pupation increased from 11 or 12 to 20 days, and the number of adults that emerged decreased from at least 70 to 0%. The growth and development of the insect may have slowed, at least in part, because this agent reduced the quantity of sterol and glyceride in the tissues of the larva. Niacin also affected the growth and development of the insect. As the concentration of niacin in the diet increased to 5.0%: the number of larval molts increased by 1, the time required for the onset of pupation increased to 21 days, pupal weight decreased significantly, but adult emergence was normal. The growth and development of the insect may have slowed, at least in part, because this agent caused sterol to accumulate in the hemolymph of the larva. A water-soluble component in the hemolymph also increased in the presence of niacin, but there was little or no change in the glyceride content. Further studies are warranted to determine the mode of action of these hypolipidemic agents in H. zea.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120404
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 68
    Electronic Resource
    Electronic Resource
    Properties, synthesis, and accumulation of storage proteins in Pieris rapae L. (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 215-228 
    Details
    ISSN: 0739-4462
    Keywords: hemolymph ; fat body ; storage granules ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Two kinds of storage proteins (SP-1, SP-2) were confirmed in hemolymph and fat body of Pieris rapae during metamorphosis. Both proteins were present in high concentrations in the hemolymph during the last larval instar. Hemolymph concentrations of SP-1 and SP-2 dropped after pupation as the proteins were being deposited in fat bodies. SP-2 is present in a larger amount than SP-1. Detailed studies on storage proteins determined their properties, mode of synthesis, and accumulation in the fat body.SP-1 has a molecular weight of 500,000 and consists of one type of subunit (Mr 77,000), while SP-2 has a molecular weight of 460,000 and is composed of two types of subunits (Mr 80,000 and 69,000). The pl values of SP-1 and SP-2 were determined to be 6.97 and 7.06, respectively.Fat body cells from 1-day-old fifth instar larvae synthesized storage proteins in large amounts, whereas those from late prepupae exhibited high protein sequestration. Proteins taken up in fat body accumulated in dense granules during the pupal stage but sharply decreased at the adult stage.Morphological changes in the fat body tissues were observed during the larval-pupal transformation; the nuclei of fat body cells became irregularly shaped, and the boundaries between cells seemed to be obscure. Synthesis, storage, or degradation of storage proteins in fat body during development is closely associated with morphological changes in the tissues.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100305
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 69
    Electronic Resource
    Electronic Resource
    Juvenile hormone identification, titer, and degradation during the last larval stadium of Spodoptera littoralis (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 1-14 
    Details
    ISSN: 0739-4462
    Keywords: esterase ; Lepidoptera ; insect development ; α-naphthyl acetate ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Juvnile hormone (JH) was identified and titers determined during the last larval stadium of the cotton leafworm Spodoptera littoralis using combined gas chromatography-selected ion monitoring-mass spectrometry. JH was almost exclusively limited to JH II, occurring at two major peaks: the first at the beginning of the stadium and the second at days 4 and 5 just after wandering. Degradation of JH and α-naphthyl acetate (α-NA) in hemolymph and fat body was determined during the same developmental periods. JH degradation in hemolymph occurred initially as a broad bimodal peak during the second half of feeding, with peaks at days 2 and 3. The second peak occurred at the end of the stadium, subsequent to the second JH II titer peak. Three α-NA esterase peaks in hemolymph were detected when JH degradation was at a very low level. Fat body JH degradation was resolved as four activity peaks throughout the stadium, with the first three peaks occurring just previous to the JH degradation peaks in the hemolymph. The highest levels of JH and α-NA degradation activities in fat body were related to the wandering stage.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120102
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 70
    Electronic Resource
    Electronic Resource
    Announcements (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 75-75 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120107
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 71
    Electronic Resource
    Electronic Resource
    Alteration of hemolymph polypeptides in Manduca sexta larvae parasitized by Cotesia congregata: A two-dimensional electrophoretic analysis and comparison with major bacteria-induced proteins (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 29-45 
    Details
    ISSN: 0739-4462
    Keywords: parasitism ; tobacco hornworm ; polyacrylamide gel electrophoresis ; hemolymph proteins ; insect defense mechanisms ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Analyses using one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) previously demonstrated that parasitization by the braconid wasp Cotesia congregata significantly alters the normal hemolymph polypeptide profile of host Manduca sexta larvae. In the present study two-dimensional gel analyses corroborated our earlier findings and provided additional evidence that multiple parasitism-specific polypeptides were induced, which varied according to the stage of development of the wasps. Parasitization additionally elicited changes in the total protein concentration detected in the blood. Initially an elevation was observed, with newly parasitized larvae exhibiting a twofold elevation in hemolymph protein concentration by 12-24 h postoviposition. In contrast, terminal-stage hosts with second instar parasites had significantly less protein in the hemolymph, likely due to reduced growth and inhibition of arylphorin synthesis by the fat body during the final stages of parasitism. Comparison of the array of hemolymph polypeptides produced in unparasitized larvae injected with 106cells of the gram-negative bacterium Enterobacter cloacae with those proteins induced by parasitization indicated the two classes are different. Our findings confirm that the hostresponse to parasitism is a specific one, and not mimicked by bacterial challenge. Duringshort-term in vitro culture of wasp larvae dissected from the host hemocoel, several proteins were detected in the medium using SDS - PAGE, with their appearance in vitro suggestive of secretion by the wasps in vivo. Moreover, hemolymph from the parasites had significant amounts of putative host proteins, including an arylphorin - like polypeptide and a protein with a mobility similar to that of insecticyanin. Thus, a dynamic interchange of proteins may occur, with the parasites accumulating host proteins while simultaneously secreting a variety of factors into the host hemocoel.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100104
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 72
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100201
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 73
    Electronic Resource
    Electronic Resource
    Complete amino acid sequence of Bombyx egg-specific protein deduced from cDNA clone (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 131-139 
    Details
    ISSN: 0739-4462
    Keywords: nucleotide sequence ; signal peptide ; serine-rich domain ; N-glycosylation sequence ; metal-binding sequence ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Complementary (c)DNA coding for an insect yolk protein, the egg-specific protein of the silkworm Bombyx mori was cloned and the nucleotide sequence determined. The sequence covers the entire coding region of 1,677 base pairs with 5′ and 3′ noncoding regions (21 and 115 base pairs, respectively). The deduced amino acid sequence of the egg-specific protein consists of 559 amino acid residues. The NH2-terminal 18 amino acid sequence is enriched in hydrophobic amino acids and assumed to be a signal peptide. A sequence, Asn-X-Thr, a potential N-linked glycosylation site, is found at positions 191 to 193. A serine-rich domain is localized in the region from 63 to 90, in which phosphorylation takes place. Cys His motif in 405 to 415 is analogous to a proposed metal binding sequence. Lys132-Asn133 and Arg228-Asp229 are probably the sites cleaved by the egg-specific protein protease that appears during embryogenesis. The derived amino acid sequence has no appreciable homology to other sequenced proteins.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100204
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 74
    Electronic Resource
    Electronic Resource
    Masthead (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100301
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 75
    Electronic Resource
    Electronic Resource
    Mediation of ecdysone synthesis in Manduca sexta by a hemolymph enzyme (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 179-197 
    Details
    ISSN: 0739-4462
    Keywords: insect molting ; tobacco hornworm ; dehydroecdysone ; ketoecdysteroid reductase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The prothoracic glands of Manduca sexta synthesize dehydroecdysone, which is rapidly converted to ecdysone through the mediation of a hemolymph enzyme, a 3 β-forming-3-ketosteroid reductase. The hemolymph protein fraction (HPF) containing this enzyme was obtained from diapausing and non-diapausing pupae, isolated abdomens, surgically manipulated pupae, etc., and in all cases had the capacity to affect the conversion of dehydroecdysone to ecdysone. The enzyme is heat labile, is inactivated by trypsin, and has a molecular weight of between 20,000 and 30,000. The data indicate that the conversion of dehydroecdysone to ecdysone exhibits linear kinetics and may be dependent on both the enzyme concentration and the concentration of NADPH at the beginning of the reaction but may be limited by the absolute amount of reducing equivalents after 10 min, under the experimental conditions utilized. The capacity of the enzyme to reduce dehydroecdysone was titered in the hemolymph during the last larval instar and during prepupal and pupal life with maximum capacity exhibited at the beginning of the instar, on day 8 of larval life and at day 1 of pupal life. Even at its lowest point at day 5, 1 ml of hemolymph was able to convert 77 pmol (∼35 ng) dehydroecdysone to ecdysone in 1 min. These results require a new interpretation of the control of molting in the Lepidoptera.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100303
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 76
    Electronic Resource
    Electronic Resource
    Possible role for covalent modification in the reversible activation of ecdysone 20-monooxygenase activity (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 241-253 
    Details
    ISSN: 0739-4462
    Keywords: ecdysteroids ; hydroxylation ; 20-hydroxyecdysone ; Spodoptera littoralis ; protein kinase ; phosphoprotein phosphatase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Evidence is presented for the reversible activation-inactivation of the microsomal ecdysone 20-monooxygenase from fat body of the cotton leafworm, Spodoptera littoralis, in a manner commensurate with reversible changes in its phosphorylation state. The activity of the monooxygenase was higher following preincubation with fluoride (an inhibitor of phosphoprotein phosphatases) than in its absence. Preincubation with alkaline phosphatase or with cAMP-dependent protein kinase resulted in appreciable diminution or enhancement, respectively, in monooxygenase activity. Activation of ecdysone 20-monooxygenase activity could also be effected by incubation with a cytosolic fraction in the presence of cAMP, ATP, and fluoride; this activation was prevented by a cAMP-dependent protein kinase inhibitor. Similarly, inactivation of the monooxygenase was achieved by preincubation with cytosol, the effect being enhanced by Ca2+-calmodulin or by Mg2+ ions. The combined results provide indirect evidence that the microsomal ecdysone 20-monooxygenase exists in an active phosphorylated form and an inactive dephosphorylated form, interconvertible by a cAMP-dependent protein kinase and a phosphoprotein phosphatase.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100307
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 77
    Electronic Resource
    Electronic Resource
    Juvenile hormone esterase activity from Manduca sexta corpora allata in vitro (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 93-108 
    Details
    ISSN: 0739-4462
    Keywords: endocrine feedback ; hemolymph JH esterase ; fluoromevalonolactone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Juvenile hormone esterase (JHE) activity released by the corpora allata (CA) into incubation media (CA-JHE) was titered daily during the course of the last (fifth [V]) larval stadium of Manduca sexta. This CA-JHE activity was relatively low during the early last stadium up to the time of commitment (V4), then rose rapidly to a peak on V6. Activity declined sharply almost to precommitment levels by V8, before rising to a second peak on the first day of the pupal phase (P0). This pattern of activity is distinct from that of hemolymph JHE activity, which peaks just prior to wandering on V4 and again just prior to pupation (V9). Although the CA-JHE and hemolymph-JHE possess different temporal patterns of activity, isoelectric focusing, gel electrophoresis, and initial studies with selected inhibitors suggest that the enzymes responsible for the CA-JHE and hemolymph-JHE activities are similar, but not identical, in nature.Exposure of the V6 CA in vitro to JH II (0.1 μM) or fluoromevalonolactone (FMev; 0.1 mM) produced an approximate fivefold increase and 60% decrease in JH acid synthesis, respectively. Conversely, the same treatments resulted in an inhibition (JH II) and stimulation (FMev) of CA-JHE activity. These observations suggest that JH may be involved in the direct positive feedback regulation of postwandering larval CA and that the CA-JHE may also be integrally related to this positive feedback mechanism.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110204
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 78
    Electronic Resource
    Electronic Resource
    Purification and characteristics of a specific alkaline phosphatase from the integument of the mediterranean fruit fly, Ceratitis capitata (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 217-230 
    Details
    ISSN: 0739-4462
    Keywords: enzyme ; Diptera ; sclerotization ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A specific alkaline phosphatase (ALPase) from the integument of white pupae has been purified 500-fold. The purification procedure included solubilization with Triton X-100, butanol extraction, fractionation with ammonium sulfate, and chromatography on concanavalin A-Sepharose, Sephadex G-200, and Sepharose 6B. Two peaks with enzyme activity were observed. The major peak had a molecular weight of approximately 180,000, while the minor peak, which had identical kinetic parameters and substrate specificity as those of the major one, was eluted in a high molecular weight form (about 900,000), probably cross-linked with chitin, since the enzyme was separated from the chitin only by lysozyme treatment. The enzyme hydrolyzes only tyrosine phosphate and β-glycerophosphate, with apparent Kms of 0.35 mM and 0.22 mM, respectively, but not serine phosphate, threonine phosphate, ATP, and AMP. The optimum pH was in the alkaline range, with a peak at pH 9.4. The divalent cations Mn2+, Mg2+, and Ba2+ had stimulatory actions, while Cu2+ exerted a very strong inhibitory action on the enzyme activity. The ALPase was inhibited by L-tyrosine in a dose-dependent fashion. At a concentration of 2 mM, L-tyrosine totally inhibited the enzyme activity, while L-phenylalanine inactivated the enzyme about 25%. The accumulated evidence that ALPase is involved in the sclerotization process of insect integument is discussed.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110403
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 79
    Electronic Resource
    Electronic Resource
    Distribution, properties, and functions of midgut carboxypeptidases and dipeptidases from Musca domestica larvae (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 231-244 
    Details
    ISSN: 0739-4462
    Keywords: midgut peptidases ; houseflies ; subcellular fractionation ; protein digestion ; membrane-bound carboxypeptidase A ; soluble carboxypeptidase A ; membrane-bound dipeptidase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Dipeptidase and carboxypeptidase A activities were determined in cells and luminal contents of the fore-, mid-, and hind-midgut of Musca domestica larvae. Dipeptidase activity was found mainly in hind-midgut cells, whereas carboxy-peptidase activity was recovered in major amounts in both cells and in luminal contents of hind-midguts. The subcellular distribution of dipeptidase and part of the carboxypeptidase A activities is similar to that of a plasma membrane enzyme marker (aminopeptidase), suggesting that these activities are bound to the microvillar membranes. Soluble carboxypeptidase A seems to occur both bound to secretory vesicles and trapped in the cell glycocalyx. Based on density-gradient ultracentrifugation and thermal inactivation, there seems to be only one molecular species of each of the following enzymes (soluble in water or solubilized in Triton X-100): membrane-bound dipeptidase (pH optimum 8.0; Km 3.7 mM GlyLeu, Mr 111,000), soluble carboxypeptidase (pH optimum 8.0; Km 1.22 mM N-carbobenzoxy-glycyl-L-phenylalanine (ZGlyPhe), Mr45,000) and membrane-bound carboxypeptidase (pH optimum 7.5, Km 2.3 mM ZGlyPhe, Mr58,000). The results suggest that protein digestion is accomplished sequentially by luminal trypsin and luminal carboxypeptidase, by membrane-bound carboxypeptidase and aminopeptidase, and finally by membrane-bound dipeptidase.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940110404
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 80
    Electronic Resource
    Electronic Resource
    Ploidy levels and DNA synthesis in fat body cells of the adult mosquito, Aedes aegypti: The role of juvenile hormone (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 133-143 
    Details
    ISSN: 0739-4462
    Keywords: microspectrophotometry ; methoprene ; egg development ; yellow fever mosquito ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Adult females of the mosquito Aedes aegypti showed two cycles of DNA replication in the fat body based on microspectrophotometric measurement of changes in nuclear DNA. The first cycle began after emergence and resulted in 80% of diploid fat body cells becoming tetraploid and 20% becoming octoploid by the end of the third day. The second replication cycle occurred 48-72 h after a blood meal and resulted in an increase in octoploid nuclei to 67% Topical application of juvenile hormone or methoprene to abdomens isolated at emergence stimulated an increase in ploidy levels above that normally seen in situ. Synthesis of DNA, estimated by incorporation of injected [3H]-thymidine, rose after emergence and remained high for 2 days. Synthesis increased again after a blood meal, reached a peak by 6 h, and returned to low levels by 24 h after the meal. The timing of DNA synthesis and a measurable increase in ploidy were temporally separated. The ploidy increase, but not DNA synthesis, was correlated with increases in juvenile hormone levels.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120302
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 81
    Electronic Resource
    Electronic Resource
    Cycles of protein synthesis during pupal diapause in the flesh fly, Sarcophaga crassipalpis (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 111-122 
    Details
    ISSN: 0739-4462
    Keywords: MO2 cycles ; juvenile hormone ; infradian cycle ; metabolism ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Protein synthesis is cyclic during pupal diapause in Sarcophaga crassipalpis. These cycles are in phase with infradian MO2 cycles, which have a periodicity of about 4 days at 25°C. Mean incorporation of [35S]methionine by diapausing pupae was 5.4% during the 2 days of highest MO2 but dropped to 1.7% during the 2 days of low MO2. Diapausing pupae treated with a juvenile hormone analog prior to pupariation had a constant high MO2 similar to peak values observed in untreated pupae, and such pupae consistently incorporated [35S]methionine at a high rate (7.7%). [35S]Methionine incorporation by nondiapausing pupae and pharate adults was eightfold higher than the peak rates observed during diapause. Autoradiography of in vivo labeled proteins indicated quantitative and qualitative changes in the synthesis of proteins by diapausing pupae during different phases of the MO2 cycle. Brains from diapausing pupae labeled in vitro showed higher incorporation at the peak of the MO2 cycle than at the nadir of the cycle, but no such differences were detected for integument, fat body, or fat body supernatant. Theses differences in tissue response indicate that control of protein synthesis during diapause is not cell autonomous, but is a function of the metabolism of the intact organism.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120205
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 82
    Electronic Resource
    Electronic Resource
    Catecholamines in the cuticles of four strains of the german cockroach Blattella germanica (L.) during sclerotization and melanization (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 12 (1989), S. 145-156 
    Details
    ISSN: 0739-4462
    Keywords: dopamine ; N-acetyldopamine ; N-β-alanyldopamine ; N-β-alanylnorepinephrine ; N-acetylnorepinephrine ; mutants ; cockroaches ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Catecholamines were extracted from the cuticles of four strains of the cockroach Blattella germanica at different times 48 h after adult ecdysis and analyzed by reverse phase HPLC with electrochemical detection. The wild (VPl), black (Bl), orange (or), and yellow (y) phenotypes differ in cuticular pigmentation, particularly in the extent of melanization. N-β-Alanyldopamine (NBAD) and N-β-alanylnorepinephrine (NBANE) were major o-diphenolic compounds in extracts from cuticle of all strains during the main period of sclerotization. N-Acetyldopamine (NADA) and N-acetylnorepinephrine (NANE) were minor the first day after ecdysis, but accumulated to higher levels thereafter. Dopamine (DA) concentrations were higher in the darker pigmented cuticles of strains Bl and or than in the lighter-colored cuticles of strains VPl and y. Extractable DA rapidly increased in VPl, Bl, and or cuticles shortly after ecdysis, reached peak levels 6-24 h later, and then decreased after melanization. Only small amounts of DA were detected in strain y cuticle, whereas NBANE concentrations were very high. Therefore, high DA levels in cuticle are correlated with melanization that occurs during the first few hours after adult ecdysis, whereas sclerotization is correlated with high levels of the N-β-alanylcatecholamines. Sclerotization appears to be delayed in strain Bl, since only low concentrations of the N-acylated catecholamines accumulate until after melanization is completed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940120303
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 83
    Electronic Resource
    Electronic Resource
    Introduction: Dedicated to Malcolm J. Thompson on the occasion of his retirement (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 177-177 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100302
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 84
    Electronic Resource
    Electronic Resource
    Mode of action of diptericin A, a bactericidal peptide induced in the hemolymph of Phormia terranovae larvae (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 229-239 
    Details
    ISSN: 0739-4462
    Keywords: insect immunity ; antibacterial protein ; bacterial cytoplasmic membrane ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Diptericin A is a member of a multigenic family of antibacterial peptides that are synthesized by larvae of Phormia terranovae (Diptera) in response to a bacterial injection or to injury. The 82-residue peptide is active only against a limited range of Gram-negative bacteria. Data presented suggest that the primary action of diptericin A is on the cytoplasmic membrane of growing bacteria.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100306
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 85
    Electronic Resource
    Electronic Resource
    20-Hydroxyecdysone and ovarian maturation in the firebrat Thermobia domestica (Thysanura: Lepismatidae) (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 7 (1988), S. 281-293 
    Details
    ISSN: 0739-4462
    Keywords: previtellogenesis ; molting cycles ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The effects of 20-hydroxyecdysone on ovary maturation in the firebrat Thermobia domestica were investigated by in vivo injections of different doses of the hormone on various days of the reproductive cycle. Several females were neck-ligated or treated with precocene II before injection. Experiments were also performed on ovarioles incubated in vitro. It was demonstrated that 20-hydroxyecdysone has direct and dose-dependent effects on the ovary, inducing growth of all the previtellogenic follicles whatever the day of the reproductive cycle, except at times when the ovaries contain follicles undergoing choriogenesis. The major effect of the hormone is the stimulation of young-follicle formation in the anterior part of the previtellarium and the accelerated growth of a set of basal previtellogenic follicles, which reach the critical size required for yolk deposition. However, 20-hydroxyecdysone did not induce cellular differentiation, in particular, the enlargement of the perioocyte space and the development of oocyte microvilli, which normally occur before yolk precursor incorporation. The present results give a better understanding of the temporal relationships between molting and reproductive cycles and also explain the periodicity of ovarian maturation.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940070406
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 86
    Electronic Resource
    Electronic Resource
    Dose-dependent influence of Campoletis sonorensis polydnavirus on the development and ecdysteroid titers of last-instar Heliothis virescens larvae (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988), S. 113-126 
    Details
    ISSN: 0739-4462
    Keywords: insect viruses ; parasitoid ; prothoracic glands ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Campoletis sonorensis calyx fluid arrests the development of last-instar Heliothis virescens larvae and is associated with the gross degeneration of the host's prothoracic glands. Through manipulations of ovary supernatant, Campoletis sonorensis polydnavirus (CsV) was found to be the only component of calyx fluid responsible for causing host developmental arrest. Venom from C. sonorensis had no effect on host development. Suspensions of CsV were quantified, and various doses were injected into last-instar hosts. The percentage of larvae developmentally arrested was dose dependent. In addition, larvae not arrested by injection with CsV suspensions were developmentally delayed in a dose-dependent manner. Hosts were delayed in the stage in which they were injected and, after recovery, developed at normal rates. Measurements by radioimmunoassay indicated that developmental delay was due to a suppression of ecdysteroid titers. After a dose-dependent period of suppression, hemolymph ecdysteroid titers recovered and reached titers comparable to those observed in saline-injected controls. Examination of prothoracic glands from developmentally delayed larvae revealed that partial degeneration occurred. Comparisons of the number and mean size of surviving gland cells and the length of developmental delay suggested that surviving gland cells may compensate for degenerated cells by increasing their ecdysone production.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940080205
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 87
    Electronic Resource
    Electronic Resource
    Neuroparsin: A new energetic neurohormone in the African locust (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988), S. 135-145 
    Details
    ISSN: 0739-4462
    Keywords: Locusta migratoria ; neuroparsin ; corpora cardiaca ; trehalose ; glycogen ; lipid ; adipokinetic hormone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The effects of neuroparsins on hemolymph trehalose and lipid levels and on total glycogen content were analyzed in Locusta migratoria. Saline and methanol extracts of the two lobes of the corpora cardiaca were assayed. Neuroparsins (A and B) were demonstrated to be hypertrehalosemic and hyperlipemic proteins of the neural lobe. Both of these metabolic activities of neuroparsins were somewhat less potent than those of adipokinetic hormone (AKH). Neuroparsin activity could be distinguished from AKH by blockage with an antiserum specific to neuroparsin. The hypertrehalosemic response induced by neuroparsins, in contrast to that of AKH, appeared to occur without a decrease of total glycogen content. The differential modes of action of AKH and neuroparsins could contribute to the fine modulation of carbohydrate metabolism in Locusta migratoria.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940080207
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 88
    Electronic Resource
    Electronic Resource
    Masthead (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940080401
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 89
    Electronic Resource
    Electronic Resource
    Quantitative determination of trypsinlike and chymotrypsinlike enzymes in insects (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988), S. 249-260 
    Details
    ISSN: 0739-4462
    Keywords: DFP ; DIP derivatives ; electrophoresis ; fluorography ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A quantitative and highly specific assay for the determination of trypsinlike and chymotrypsinlike enzymes in insects has been developed. The assay is based on the specific binding of [1,3-3H]diisopropylfluorophosphate to trypsinlike and chymotrypsinlike enzymes. Trypsinlike enzymes can be determined specifically in the presence of 10 mM TPCK (tosylamide-2-phenylethyl chloromethyl ketone; chymotrypsin inhibitor) and chymotrypsinlike enzymes can be determined in the presence of 10 mM TLCK (tosyl-L-lysine chloromethyl ketone HCI; trypsin inhibitor). The assay can easily detect 65 ng of either trypsinlike or chymotrypsinlike enzymes in midgut homogenates or whole extracts of many insect species. Using this assay, we have determined the amount of trypsinlike equivalents in Phlebotomus papatasi, Pediculus humanus, Stomoxys calcitrans, Musca domestica, Leishmania major promastigotes, Aedes aegypti, Culex nigripalpus, Culex quinquefasciatus, and Culicoides variipennis. No trypsinlike equivalents were found in Rhodnius prolixus or Ornithodoros moubata. The assay is useful for comparative studies and can be expanded for use as an electrophoretic fluorographic tool in the study of trypsinlike and chymotrypsinlike isozymes.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940080406
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 90
    Electronic Resource
    Electronic Resource
    Gene structure, cDNA sequence, and developmental regulation of a low molecular weight hemolymph protein from Locusta migratoria (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988), S. 203-217 
    Details
    ISSN: 0739-4462
    Keywords: fat body ; insect gene ; juvenile hormone ; locust ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: From a Locusta migratoria genomic DNA library, a gene has been isolated that codes for a previously unrecognized hemolymph protein of Mr = 19,000, designated 19k protein. The gene has at least five exons, extending over about 9 kb of DNA. Its polypeptide product, obtained by cell-free translation of mRNA selected from adult fat body RNA by hybridization with the cloned DNA, is precipitated by antiserum against a low molecular weight hemolymph protein fraction. The mature protein product has been purified from locust hemolymph, and an N-terminal sequence of 20 amino acids has been determined. In polyacrylamide gel electrophoresis, this protein comigrates with apolipophorin III, from which it was previously not distinguished, but it is clearly distinct by amino acid composition and sequence. The genomic clone was used as a probe to isolate a fat body cDNA clone of the 19k protein mRNA. The 938-base pair cDNA clone contains a 516-base pair open reading frame. The deduced 172-amino acid polypeptide includes an apparent signal peptide, a sequence of four amino acids that may represent a prosegment, and a sequence identical (with a single exception, which may reflect polymorphism) with the N-terminal sequence of the hemolymph protein. Its mRNA occurs at a low level in late larval fat body, is abundant in the newly eclosed adult, then declines to a low level, and rises again at days 8-10; it is greatly reduced after destruction of the corpora allata with precocene and then is elevated after treatment with methoprene, suggesting stimulation by juvenile hormone. The biological role of 19k protein is unknown.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940080402
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 91
    Electronic Resource
    Electronic Resource
    Identification and characterization of a novel postlarval hemolymph protein from Manduca sexta (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 81-90 
    Details
    ISSN: 0739-4462
    Keywords: Manduca sexta ; hemolymph ; postlarval ; protein ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The identification, purification and characterization of a new postlarval specific hemolymph protein from Manduca sexta is described. Incorporation of [35S]methionine into Manduca sexta hemolymph proteins in vivo was investigated as a function of development. A major protein band of Mr ≈ 50,000 was highly labeled during the prepupal and adult stage but not in feeding larvae. This postlarval protein (PLP) was isolated from adult male hemolymph and its chemical and immunological properties determined. PLP is a basic protein (pI ∼8.6). Electrophoresis under denaturing conditions reveals a subunit Mr ≈ 50,000 while the native protein has an apparent Mr ∼ 85,000 by gel permeation chromatography. Anti-PLP serum recognized PLP but not other hemolymph proteins on immunoblots. In vitro translation of fat body mRNA followed by immunoprecipitation revealed that fat body is the site of PLP synthesis. Quantitation of PLP levels in hemolymph throughout development was performed and suggests PLP may play a role in adult development of M. sexta.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940090202
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 92
    Electronic Resource
    Electronic Resource
    Inositol phospholipid hydrolysis may mediate the action of proctolin on insect visceral muscle (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 201-209 
    Details
    ISSN: 0739-4462
    Keywords: inositol phosphates ; phorbol esters ; diacylglycerol analogue ; oviduct ; locust ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The formation of inositol phosphates in response to the neuropeptide proctolin was studied in locust oviducts. Glycerophosphoinositol, inositol 1-phosphate, inositol 1,4-bisphosphate, and inositol 1,4,5-trisphosphate were identified in the locust oviducts using anion-exchange chromatography. Proctolin stimulated the release of inositol 1-phosphate, inositol 1,4-bisphosphate, and inositol 1,4,5-trisphosphate during a 5-min incubation. In the presence of lithium ions the effects of proctolin were enhanced, with elevations of 98%, 42%, and 45% of inositol 1-phosphate, inositol 1,4-bisphosphate, and inositol 1,4,5-trisphosphate, respectively.Physiologically the effects of proctolin upon muscular contraction of locust oviducts were mimicked by the active phorbol ester, phorbol 12-myristate 13-acetate, and by the diacylglycerol analogue, 1-oleoyl-2-acetylglycerol. The inactive phorbol ester, 12-myristate 13-acetate 4-O-methyl ether, was without effect. The effects of the active phorbol ester and the diacylglycerol analogue were calcium-dependent requiring micromolar concentrations of calcium.The results indicate that the locust oviducts possess proctolin receptors that are linked to phosphatidylinositol metabolism and that inositol phospholipid hydrolysis may mediate the physiological action of proctolin.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940090304
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 93
    Electronic Resource
    Electronic Resource
    Polypeptide composition and biosynthesis of the yolk proteins in the firebrat, Thermobia domestica (insecta, thysanura) (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 299-312 
    Details
    ISSN: 0739-4462
    Keywords: polypeptides ; immunology ; pulse-chase ; processing ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Ion-exchange chromatography of crude ovarian extracts of the primitive insect Thermobia domestica allowed the separation, in native conditions, of major and minor vitellins of molecular weights of 300,000 and 430,000, respectively. Their polypeptide subunits were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunotransfer using an antiserum prepared against major vitellin. This protein was resolved into large (Mr 166,000-212,000) and small (around Mr 50,000) polypeptides. Minor vitellin, on the other hand, exclusively contained small polypeptides that are immunologically different from those of the major vitellin. Vitellogenin polypeptides from the hemolymph of mature females exhibited electrophoretic mobilities and immunological properties similar to vitellin polypeptides. Pulse-chase experiments showed that the female fat body synthesizes radioactive and immunoprecipitable proteins, whose polypeptide pattern is close to that of the major vitellogenin. However, part of the primary vitellogenic polypeptides, at Mr 210,000 and 212,000, is rapidly processed to Mr 176,000 and 182,000 subunits. These two polypeptides, as well as the precursors, enter into the composition of the major hemolymph vitellogenin. Finally, processing of the still uncleaved 210,000-212,000 polypeptides takes place in the ovary, which performs the same step of vitellogenin maturation as the fat body.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940090405
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 94
    Electronic Resource
    Electronic Resource
    Adsorptive endocytosis of vitellogenin, lipophorin, and microvitellogenin during yolk formation in Hyalophora (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 339-355 
    Details
    ISSN: 0739-4462
    Keywords: cecropia ; hemolymph proteins ; inulin ; vitellogenesis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Yolk in Hyalophora cecropia is a mixture of proteins that are derived from the extracellular medium. We have measured for five of these proteins the number of moles deposited in each egg, the molarity of their precursors in the hemolymph at a midpoint in vitellogenesis (day 18 of adult development), and the degree to which they are concentrated by the oocyte, relative to inulin. The proteins were isolated by gel permeation and ion exchange chromatography and used to generate antibodies in rabbits. Preliminary studies established that yolk proteins are essentially quantitatively extractable in media suitable for measuring antigen concentrations by precipitation with antibodies and that yolk and hemolymph forms of the five proteins have, effectively, the same antibody-binding specificities as the isolated standards. Content per egg was about 900 pmol for vitellogenin, 600 pmol for microvitellogenin, and 300 pmol for lipophorin. By contrast, two hemolymph storage hexamers, arylphorin and a flavoprotein, occurred at less than 3 pmol per egg. In principle, yolk precursors are taken in both as solutes in the fluid phase of the endocytotic vesicles and as ligands adsorbed to vesicle membranes. Measurements of inulin uptake indicated that fluid phase endocytosis could account for only 4% of vitellogenin, 1% of microvitellogenin, and 15% of lipophorin in the yolk, when hemolymph precursors are at their day 18 concentrations. By the same comparison, arylphorin and flavoprotein appear to be excluded from the yolk, relative to inulin.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940090408
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 95
    Electronic Resource
    Electronic Resource
    Profile of free and conjugated ecdysteroids and ecdysteroid acids during embryonic development of Manduca sexta (L.) following maternal incorporation of [14C]cholesterol (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 7 (1988), S. 157-172 
    Details
    ISSN: 0739-4462
    Keywords: radiolabeled ecdysteroids ; conjugates ; 26-hydroxyecdysone 22-glucoside ; 26-hydroxyecdysone 26-phosphate ; 26-hydroxyecdysone ; 20-26-dihydroxyecdysone ; 3-epi-20-26-dihydroxyecdysone ; 3-epi-20-hydroxyecdysonoic-acid ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The levels of both free and conjugated ecdysteroids, maternally labeled from [14C]cholesterol, of six different age groups of Manduca sexta eggs were quantitatively determined. Eggs 0-1-h old contain about 2.5 and 35 μ/g of the 2- and 26-phosphates of 26-hydroxyecdysone, respectively, and 1 μg/g of 26-hydroxyecdysone. During embryogenesis of 26-hydroxyedcdysone 26-phosphate is hydrolyzed to 26-hydroxyecdysone, which reaches a peak titer in 1-18-h-old eggs; the level of 26-hydroxyecdysone 2-phosphate remains rather constant. Additionally, other metabolic modifications such as hydroxylation, conjugation, epimerization, and oxidation are occurring; and as the level of the 26-hydroxyecdysone 26-phosphate decreases there is a progression of other ecdysteroids. C-20 hydroxylation first appears in 24-40-h-old eggs and reaches peak activity in 48-64-h-old eggs, where 20-hydroxyecdysone and 20, 26-dihydroxyecdysone are both present at peak titer but the latter is the major free ecdysteroid. Ecdysone is observed at measurable levels only in the three age groups of eggs between 1 and 64 h-old. C-3 epimerase activity also appears at 24-40 h and continually increases throughout embryogenesis to the point that 3-epi-26-hydroxyecdysone and 3-epi-20, 26-dihydroxyecdysone are the major free ecdysteroids in 96-h-old eggs. A new ecdysteroid conjugate, 26-hydroxyecdysone 22-glucoside, first appears at 24-40h and becomes the major conjugate in 72-80-h-old eggs; it represents an apparent end-product as its peak titer is reached and maintained throughout the final embryonic stages. 20-Hydroxyecdysonoic acid occurs in 48-64-h-old eggs, and along with 3-epi-20-hydroxyecdysonoic and ecdysonoic acids in 72-88-h-old eggs. 20-Hydroxyecdysonoic acid peaks during the latter time interval, and as its titer subsequently falls, there is a concurrent increase in the level of 3-epi-20-hydroxyecdysonoic which was identified as the second major component of the ecdysteroid conjugate fraction of 0-1-h-old larvae. Our results indicate that there is little or no biosynthesis of ecdysteroids during embryogenesis; that the materal ecdysteroid conjugate 26-hydroxyecdysone 26-phosphate serves as source for 26-hydroxyecdysone and the numerous metabolites; that 26-hydroxyecdysone and 20,26-dihydroxyecdysone may be the active hormones during embryonic development; and that glucosylation, epimerization, and formation of acids cosntitute inactivation processes. A scheme of the proposed pathways involved in the metabolism of 26-hydroxyecdysone 26-phosphate in the developing eggs of m. sexta is presented.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940070303
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 96
    Electronic Resource
    Electronic Resource
    Oostatic hormone inhibits biosynthesis of midgut proteolytic enzymes and egg development in mosquitoes (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 7 (1988), S. 187-210 
    Details
    ISSN: 0739-4462
    Keywords: vitellogenin ; protease ; trypsin ; inhibitors ; electrophoresis ; flurography ; ecdysteroids ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Injection of partially purified oostatic hormone (0.7 μg) into female Aedes aegypti inhibited egg development, proteolytic enzyme activity, and blood digestion in the midgut, whereas control injections of saline or insulin chain A (0.7 μg) did not affect these processes. Oostatic hormone given by enema, on the other hand, did not inhibit proteolytic enzyme activity, indicating that the hormone acts outside the midgut. A single injection of oostatic hormone (0.7 μg) caused a 1.7-1.5-fold reduction in activity of trypsinlike enzymes during blood digestion, with a 10-h delay in peak activity.Using [1,3-3H]diisopropylfluorophosphate (DFP) in the presence of 8 mM tosylamide-2-phenylethyl chloromethyl ketone, the synthesis of trypsinlike derivatives was followed in the midgut of female A. aegypti. A 4-fold reduction in [1,3-3H]diisopropylphosphoryl-trypsinlike derivatives was noted after oostatic hormone treatment. Several isozymes that are normally synthesized were absent in the presence of DFP, as assessed by polyacrylamide gel electrophoresis. Injection of oostatic hormone into decapitated and ovariectomized females that did not synthesize ecdysteroids inhibited trypsinlike enzyme synthesis and blood digestion in the midgut, indicating that oostatic hormone inhibits the midgut cells and not the ovary or the brain's endocrine system.Comparison between oostatic hormone and soybean trypsin inhibitor indicated that the former inhibited trypsin synthesis whereas the latter inhibited trypsin activity. A. aegypti oostatic hormone is not species specific and injections of the hormone into Culex quinquefasciatus, Culex nigripalpus, and Anopheles albimanus caused inhibition of egg development, blood digestion, and synthesis of trypsinlike enzymes. A direct relation between oostatic hormone synthesis and the regulation of trypsinlike activity in the midgut is proposed.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940070305
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 97
    Electronic Resource
    Electronic Resource
    Masthead (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940080101
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 98
    Electronic Resource
    Electronic Resource
    Juvenile hormone-binding protein and juvenile hormone esterase activity in hemolymph from last-instar nymphs of Leucophaea maderae (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988), S. 11-23 
    Details
    ISSN: 0739-4462
    Keywords: juvenile hormone esterase ; juvenile hormone-binding protein ; JH esterase and JH binder interaction ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The concentration of the juvenile hormone-binding protein (JHB) in hemolymph was determined throughout the last nymphal instar. It was found to be 3.9 μM at the molt to the instar, rising to 13 μM by mid-instar, and dropping to 6.7μM the day before emergence. Endocrine control of its production during the last nymphal instar could not be established. The apparent juvenile hormone esterase (JHF) activity was low at the molt to the last instar, but rose about fivefold by mid-instar, and then modestly declined. On the day of emergence, JHF activity rose to the highest level observed. A four- to fivefold increase in absolute JHF activity was determined during the first half of the last nymphal instar. This increase is not regulated by JH. Removal of the JHB from hemolymph samples by precipitation with a polyclonal specific antibody increased the JHF activity up to 1,000-fold. Thus, changes in the concentrations of JHB can affect the apparent activity of JHE, which is unrelated to the production or degradation of the JHF.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940080103
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 99
    Electronic Resource
    Electronic Resource
    On the mechanism of formation of N-acetyldopamine quinone methide in insect cuticle (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 269-281 
    Details
    ISSN: 0739-4462
    Keywords: phenoloxidase ; quinone methide isomerase ; sclerotization ; tanning ; tautomerization of quinones ; Manduca sexta ; Periplaneta americana ; Sarcophaga bullata ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The mechanism of formation of quinone methide from the sclerotizing precursor N-acetyldopamine (NADA) was studied using three different cuticular enzyme systems viz. Sarcophaga bullata larval cuticle, Manduca sexta pharate pupae, and Periplaneta americana presclerotized adult cuticle. All three cuticular samples readily oxidized NADA. During the enzyme-catalyzed oxidation, the majority of NADA oxidized became bound covalently to the cuticle through the side chain with the retention of o-diphenolic function, while a minor amount was recovered as N-acetylnorepinephrine (NANE). Cuticle treated with NADA readily released 2-hydroxy-3′,4′-dihydroxyacetophenone on mild acid hydrolysis confirming the operation of quinone methide sclerotization. Attempts to demonstrate the direct formation of NADA-quinone methide by trapping experiments with N-acetylcysteine surprisingly yielded NADA-quinone-N-acetylcysteine adduct rather than the expected NADA-quinone methide-N-acetylcysteine adduct. These results are indicative of NADA oxidation to NADA-quinone and its subsequent isomerization to NADA-quinone methide. Accordingly, all three cuticular samples exhibited the presence of an isomerase, which catalyzed the conversion of NADA-quinone to NADA-quinone methide as evidenced by the formation of NANE - the water adduct of quinone methide. Thus, in association with phenoloxidase, newly discovered quinone methide isomerase seems to generate quinone methides and provide them for quinone methide sclerotization.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940090403
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 100
    Electronic Resource
    Electronic Resource
    Vitellogenesis and oocyte development in azadirachtin-induced fifth-instar overage nymphs of Locusta migratoria (L.) (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 313-322 
    Details
    ISSN: 0739-4462
    Keywords: vitellogenin ; ovaries ; hemolymph ; fat body ; reproduction ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Injection of azadirachtin into females of Locusta migratoria at the beginning of the last nymphal instar prevented molting to the adult stage, and many of these locusts survived for long periods as overage fifth-instar nymphs. Overage female nymphs synthesized vitellogenin; maximum vitellogenin content in their hemolymph was 6-7 times higher than that found in normal adult females. The overage female nymphs developed vitellogenic oocytes, but development was retarded to some extent: although vitellogenin did accumulate in the proximal oocytes, their maximum average length was only about 2.8 mm (compared to 6.2 mm in normal adult females) and extensive oocyte resorption was observed. Thus, attainment of adult competence of the organs and processes involved in female reproduction is independent to a considerable extent from the process of overt adult morphogenesis.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940090406
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...