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  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
  • Wiley-Blackwell  (37)
  • American Meteorological Society
  • Elsevier
  • MDPI Publishing
  • 1985-1989  (37)
  • 1985  (37)
Collection
Keywords
Publisher
  • Wiley-Blackwell  (37)
  • American Meteorological Society
  • Elsevier
  • MDPI Publishing
Years
  • 1985-1989  (37)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Biosynthesis of Drosophila yolk polypeptides (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 7-27 
    Details
    ISSN: 0739-4462
    Keywords: vitellogenin ; posttranslational processing ; protein secretion ; endocytosis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The three yolk polypeptides (YPs) of Drosophila are synthesized and secreted by female fat body and ovarian follicle cells, sequestered by pinocytosis into oocytes, and finally deposited into yolk granules. The biosynthesis of the YPs was studied using two-dimensional gels. Labeling the YPs with [35S]-cysteine, an amino acid found only near the amino terminus of YP1 and YP2, showed that an amino terminal peptide is removed from YP1 and YP2 shortly after or during translation.Intermediates in YP biosynthesis corresponding in electrophoretic mobility to pancreatic membrane-processed primary translation products were also detected in a 5-min pulse label with [35S]-methionine. Genetic variants that alter YP structure were used to identify which YP precursor comes from which Yp gene. Pulse labeling with [35S]-methionine revealed that all three YPs becomes more negatively charged, that YP1 and YP2 become heterogeneously charged, and that YP1 gains in apparent molecular weight within 15 min after translation.Injecting female flies with radioiabeled sugars or orthophosphate revealed that the YPs are glycosylated and phosphorylated. Treating hemolymph proteins with phosphatase showed that phosphorylation is responsible for much of the change in charge and increase in molecular weight of the maturing YPs. These experiments with wild-type flies provide a basis for the analysis of mutations at the Yp genes which alter the structure of individual YPs.
    Additional Material: 11 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020103
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  • 2
    Electronic Resource
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    Agonistic action of synthetic analogues of quisqualic acid at the insect neuromuscular junction (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 65-73 
    Details
    ISSN: 0739-4462
    Keywords: amino acid receptors ; mealworm muscle ; new agonists ; quisqualate analogues ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: One hundred twenty analogues of quisqualic acid were synthesized and assayed on the neuromuscular junction of larva of the mealworm, Tenebrio molitor. Two new agonists for amino acid receptors, L-glutamic acid N-thiocarboxyanhydride (L-GANTA) and DL-hydantoinpropionic acid (DL-HPA), were discovered in this study. L-GANTA and DL-HPA produced muscle membrane depolarization, accompanied by a reduction of the muscle input resistance. The amplitude of excitatory postsynaptic potentials was decreased in the presence of L-GANTA and DL-HPA. The apparent dissociation constants obtained from dose-depolarization plots were 7 x 10-4 M for L-GANTA and 9 x 10-4 M for DL-HPA. Some structural constraints imposed on agonists at amino acid receptors on insect muscle were discussed.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020107
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  • 3
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    Rapid in vitro activation of corpora allata by extracted locust brain allatotropic factor (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 117-129 
    Details
    ISSN: 0739-4462
    Keywords: corpora allata ; corpora cardiaca ; juvenile hormone ; allatotropin ; Locusta migratoria ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Brains of young (newly emerged) adult female locusts (Locusta migratoria migratorioides) and of mature (〉 9 days old) locusts contain an extractable allatotropic factor, soluble in 100% methanol and in distilled water. This factor stimulates juvenile hormone III (JH III) synthesis and release from corpora allata (CA) that have been excised from donor locusts and then incubated with (radiolabeled methyl)-methionine in vitro in its presence. In addition to JH III, which is the major product synthesized by the CA, other hexanesoluble, radiolabeled compounds--more polar than JH III--are also released when CA are incubated in vitro. The activation of CA by the allatotropic factor is rapid and quickly declines when the factor is removed from the medium. Corpora allata excised from young females are marginally active and can be activated by brain allatotropic factor to less of an extent than CA of mature locusts. The content of allatotropic factor in brains of mature locusts is higher than that ascertained in brains of young females. Allatotropic factor is also present in the corpora cardiaca.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020202
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  • 4
    Electronic Resource
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    Binding of [3H]phencyclidine to membranes from housefly thoracic muscles (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 181-190 
    Details
    ISSN: 0739-4462
    Keywords: housefly muscle ; phencyclidine ; calcium channel antagonists ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The binding of [3H]phencyclidine ([3H]PCP) to a preparation of housefly thoracic muscle membranes was studied. Specific [3H]PCP binding saturated with both time and at concentrations of the radiolabeled ligand greater than 20 nM. One binding site with a KD of 10.7 nM and a Bmax of 3.9 pmol/mg protein was observed. Specific [3H]PCP binding was also readily reversible with a half-time of dissociation (t1/2) of 13.8 min and varied proportionately with tissue concentration. Of the drugs tested, specific [3H]PCP binding was inhibited by PCP analogs, antipsychotics, antidepressants, Ca2+ channel antagonists, and K+ channel blockers. [3H]PCP binding was unaffected by addition of carbamylcholine or L-glutamate in absence or presence of ATP, GTP, cAMP, or cGMP. Though the identity of the [3H]PCP binding protein in housefly muscle membranes is still unclear, it is more likely to be an ionic channel such as K+ or Ca2+ channels than a neurotransmitter receptor.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020206
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  • 5
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    Host-plant resistance of sorghum: Differential hydrolysis of sorghum pectic substances by polysaccharases of greenbug biotypes (Schizaphis graminum, homoptera: Aphididae) (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 203-215 
    Details
    ISSN: 0739-4462
    Keywords: greenbug ; Schizaphis ; biotype ; polysaccharases ; probing behavior ; cellulase ; pectinase ; sorghum ; symbiotes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Pectic substances extracted from different varieties of sorghum are hydrolyzed at differing rates by unfractionated polysaccharases isolated from two biotypes (C, GBC; and E, GBE) of the sorghum pest, Schizaphis graminum (the greenbug). A higher degree of susceptibility of a sorghum variety is associated with a greater rate of hydrolysis of sorghum pectic substances by a greenbug biotype. Increases in the specific activity of polysaccharases on the pectic substances from a resistant sorghum variety are dependent on the duration that a biotype is maintained as a colony on that variety. Polysaccharase activity of GBE on arabinogalactan was significantly greater than GBC. However, there were no differences between the biotypes on the depolymerization of a variety of other plant matrix polysaccharides and a synthetic polysaccharide. The sequence of substrates of increasing refractoriness to hydrolysis are: arabinogalactan 〈 microcrystalline cellulose 〈 xylan 〈 pectin 〈 2,3-diacetyl pectin 〈 α-1,4-galacturonan. Pectic substances from sorghum varieties resistant to GBC but susceptible to GBE are relatively lower in arabinogalactan with elevated levels of uronic acid (UA) compared to varieties susceptible to both biotypes. A sorghum variety resistant to both GBC and GBE was lowest in levels of arabinogalactan, highest in UA, and highest in fructan content, which in the other varieties occurred only in trace amounts. Pectic composition of rhamnose, xylose, and glucose showed no relationship to resistance. Bound phenolics (potential inhibitors of enzyme activity) were not detected in any of the sorghum pectic substances. The relationship of plant matrix polysaccharides to host-plant aphid biotype compatibility is discussed.
    Additional Material: 2 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020208
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  • 6
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    Purification and partial characterization of mosquito egg development neurosecretory hormone: Evidence for gonadotropic and steroidogenic effects (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 265-281 
    Details
    ISSN: 0739-4462
    Keywords: Aedes aegypti ; Aedes taeniorhynchus ; Aedes atropalpus ; JH ; 20-hyroxyecdysone ; egg development neurosecretory hormone ; column chromatography ; electrophoresis ; HPLC ; vitellogenesis ; tissue culture ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Egg development neurosecretory hormone (EDNH), a hormone that stimulates vitellogenesis in mosquitoes, was purified 10,000-fold from the mosquito Aedes aegypti. The purification procedure included chromatography on hydrophobic, ion exchange, and gel filtration columns, and preparative electrophoresis to give an almost homogeneous preparation. The hormone is a polypeptide monomer of molecular weight of 18,700 ± 500 as determined from SDS electrophoresis and gel filtration chromatography. Using lowpressure chromatography throughout the purification procedure, the hormone was recovered at a high yield (39%). The amount of EDNH in a mosquito is about 0.6-1.6 ng, corresponding to 32-85 fmol.Injection of purified EDNH into female mosquitoes resulted in the conversion of [14C]cholesterol into labeled ecdysone and 20-hydroxyecdysone which were separated and identified using thin-layer chromatography and high-performance liquid chromatography separation procedures.Egg development and vitellogenin synthesis were also induced when EDNH was injected into several mosquito species, indicating that the hormone is not species-specific.This report is the first to show that a purified preparation of EDNH has both steroidogenic and a gonadotropic effects on female mosquitoes.
    Additional Material: 8 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020305
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  • 7
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    Meeting announcements (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 331-331 
    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.940020309
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  • 8
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    Purification, partial characterization, and postembryonic levels of amylases from Sitophilus oryzae and Sitophilus granarius (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 415-428 
    Details
    ISSN: 0739-4462
    Keywords: Sitophilus ; S. oryzae ; S. granarius ; S. zeamais ; rice weevil ; granary weevil ; maize weevil ; amylase ; purification ; digestion ; cereals ; feeding ; amylase inhibitors ; adaptive significance ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Amylases from adults of Sitophilus oryzae (L.) and S. granarius (L.) were purified by using a sequential procedure of ammonium sulfate precipitation, glycogen-complex formation, and ion exchange chromatography. Amylase of S. oryaze was purified 47.4-fold to a specific activity of 478 units/mg protein. One amylase unit equals 1 mg maltose hydrate produced/min at 30°C. Amylase of S. granarius was purified 85.4-fold to a specific activity of 453 units/mg protein. Amylase of S. oryzae had a Km of 0.173% for soluble starch and consisted of two anionic isozyrnes with isoelectric points of pH 3.70 and pH 3.76. Amylase of S. granarius had a Km of 0.078% for starch and was a single protein with an isoelectric point of pH 3.76. Purified amylases of both species had molecular weights of 56,000 estimated by sodium dodecyl sulfatepolyacrylamide gel electrophoresis, were activated by chloride, and had double energies of activation calculated from Arrhenius plots. Based on fresh weights of adults feeding on whole wheat through 10 weeks of age, S. oryzae contained three-fold and eight-fold more amylase than S. granarius and S. zeamais Motschulsky, respectively. High amylase levels in S. oryzae may provide this species with an adaptive advantage when feeding on cereals containing naturally occurring amylase inhibitors.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020409
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  • 9
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    Critical roles for juvenile hormone and its esterase+ in the prepupa of Trichoplusia ni (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 397-404 
    Details
    ISSN: 0739-4462
    Keywords: Trichoplusia ni ; allatectomy ; juvenile hormone ; juvenile hormone esterase ; esterase inhibition ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the caterpillar Trichoplusia ni (Lepidoptera: Noctuidae) it has been demonstrated by allatectomy that the appearance of juvenile hormone during the prepupal stage is crucial for the successful larval-pupal ecdysis of most larvae. Application of juvenile hormone or juvenile hormone esterase inhibitors at key times disrupted normal development as well. Thus the subsequent disappearance of juvenile hormone is regulated by degradation by juvenile hormone esterase in addition to a hypothetical reduction in biosynthesis. This reduction in juvenile hormone titer in the prepupa is just as critical for normal development as was its previous appearance. These observations on the critical role of juvenile hormone in the prepupa are in contrast to observations in some other species. For instance, in the case of Manduca sexta (Lepidoptera: Sphingidae), juvenile hormone is considered only supplementary to the action of prothoracicotropic hormone in the postwandering stage and primarily is required for normal pupal development. It thus appears that even within the Lepidoptera the role of juvenile hormone in prepupal development can vary dramatically.
    Additional Material: 2 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020407
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  • 10
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    Meeting announcements (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 431-431 
    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.940020410
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  • 11
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    The mechanism of block of glutamate synapses by dipicolinic acid (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 1-6 
    Details
    ISSN: 0739-4462
    Keywords: dipicolinic acid ; glutamate synapse ; neuromuscular junction ; transmitter release ; Tenebrio molitor ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The effect of dipicolinic acid (2,6-pyridine dicarboxylic acid) on the mealworm neuromuscular junction was studied using conventional microelectrode recording techniques. Dipicolinic acid (10-5-10-3 M) added to the bathing solution reversibly blocked neuromuscular transmission. The depolarization in response to iontophoretically applied L-glutamate (glutamate potential) was not affected by dipicolinic acid even when the neurally evoked excitatory postsynaptic potential (EPSP) was totally abolished. Focal extracellular recordings from single synaptic sites revealed that in the presence of 1 x 10-4 M dipicolinic acid the presynaptic spike was unchanged, but the quantal content for evoked transmitter release was reduced. The calcium-dependent action potential elicited by direct stimulation of the muscle fiber was not impaired by dipicolinic acid. These results suggest that dipicolinic acid interferes with the transmitter-releasing mechanism from the presynaptic terminal.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020102
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  • 12
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    Comparative studies on pharmacokinetics and metabolism of the anti-juvenile hormone precocene II (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 55-63 
    Details
    ISSN: 0739-4462
    Keywords: precocene II ; pharmacokinetics ; detoxification ; cytochrome P-450 ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The cuticular penetration and pharmacokinetics of the anti-juvenile hormone precocene II were determined in a sensitive species (Oncopeltus fasciatus) and an insensitive species (Heliothis zea). Precocene was sequestered by the fat body and slowly metabolized in Oncopeltus, but rapidly metabolized and excreted in Heliothis. Studies in vitro using inhibitors for cytochrome P-450 and for cyt P-450-NADPH-reductase, confirmed the anticipated detoxification of precocene by a mixed-function oxidase via the 3,4-epoxide. Use of the inhibitors in vivo had no influence on the metabolism of precocene.
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020106
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  • 13
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    Effect of metamorphosis on the major hemolymph proteins of the silkworm (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 91-104 
    Details
    ISSN: 0739-4462
    Keywords: Bombyx mori ; major hemolymph protein ; metamorphosis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: During the metamorphosis of the silkworm, Bombyx mori, three major hemolymph proteins (MHPs) (molecular weights 17,000, 25,000, 27,000) were detected and found to be distributed in the hemolymph and in the tissues of several organs, such as the fat body, midgut, ovary, testis, and even eggs. The MHPs in eggs gradually decreased and disappeared during embryogenesis. The formation, distribution, and utilization of MHPs in tissues other than the gonad, however, were not affected by sex.Radioisotope experiments in vivo revealed that the MHPs were synthesized at an early period of the fifth larval instar. The synthesis of at least two of them occurred in the fat body. MHPs in the hemolymph entered the tissues at the onset of the larval-pupal transformation. On the basis of their appearance, distribution, and depletion, the MHPs may be classified as reserve proteins which are synthesized in the larval stage and utilized later in the developmental stages.
    Additional Material: 11 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020109
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  • 14
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    Juvenile hormone acid methyltransferase activity in imaginal discs of Manduca sexta prepupae (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 191-202 
    Details
    ISSN: 0739-4462
    Keywords: juvenile hormone acid methyltransferase ; juvenile hormone acid ; juvenile hormone ; imaginal disc ; Manduca sexta ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The occurrence of a peak of juvenile hormone (JH) during the prepupal period has been noted in several lepidopterans. In Manduca sexta and Hyalophora cecropia this peak is known to prevent the precocious onset of adult differentiation in imaginal tissues. However, it has previously been observed in our laboratory that corpora allata (CA) of this age are incapable of making JH owing to a lack of the terminal synthetic enzyme, juvenile hormone acid methyltransferase (JHAMT). Since the CA are required for normal pupation, it is likely that JH acid is the product released by the prepupal CA. Therefore, we analyzed whether JH acid treatment would prevent precocious adultoid differentiation in allatectomized M. sexta larvae. JH acid injections were found to be as effective as JH in normalizing pupation, and acted in a time- and dose-dependent manner. This finding led to a question of whether injected or endogenous JH acid could be methylated to JH. Homogenates of several tissues from prepupae were assayed for the presence of JHAMT. Of the tissues assayed, only imaginal discs possessed significant levels of the enzyme. These results support our previously proposed mechanism for production of the prepupal JH peak in M. sexta.
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    URL: http://dx.doi.org/10.1002/arch.940020207
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  • 15
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    Comparative studies on ecdysone metabolism between mature larvae and pharate pupae in the fleshfly, Sarcophaga peregrina (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 237-250 
    Details
    ISSN: 0739-4462
    Keywords: ecdysone ; 20-hydroxyecdysone ; inactivation ; conjugate ; ecdysonoic acids ; Sarcophaga ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Metabolites of radioactive ecdysone or 20-hydroxyecdysone in larvae and pharate pupae of Sarcophaga peregrina were separated and identified by using thin-layer chromatography, high-performance liquid chromatography, and chemical methods. At the larval stage ecdysone was metabolized to biologically less active ecdysteroids predominantly through 20-hydroxyecydsone, at the pharate pupal stage, to other ecdysteroids which were tentatively identified as 26-hydroxyecdysone, 3-epi-26-hydroxyecdysone, and 3-epi-20,26-dihydroxyecdysone. Ecdysteroid acids were found in the polar metabolites during pharate pupal-pupal transformation, but scarcely detected in the larval metabolites. These acids were presumed to be ecdysonoic acid, 20-hydroxyecdysonoic acid, and their epimers. The conjugates of ecdysteroid that released the free ecdysteroids by enzymatic hydrolysis were produced more in larvae than in pupae, whereas the very polar ecdysteroids that were not affected by the enzyme were found more in pupae. Therefore, there are different metabolic pathways of ecdysone between these two successive developmental stages, and the alteration of the metabolic pathway may serve as one of the important factors in a regulatory mechanism of molting hormone activity which is responsible for normal development of this insect.
    Additional Material: 8 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940020303
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  • 16
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    Masthead (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985) 
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    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.940020401
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  • 17
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    Vitamin C enhancement of brood rearing by caged honeybees fed a chemically defined diet (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 29-37 
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    ISSN: 0739-4462
    Keywords: ascorbic acid ; dehydroascorbic acid ; vitamin C ; honeybees ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Pollen collected by bees was sampled during a 3-h period once a week from April to October 1983 and analyzed for vitamin C (L-ascorbic acid and dehydroascorbic acid). The levels were highly variable and ranged from a low of 136 μg/g pollen (April) to a high of 1943 μg/g pollen (May). Overall, caged honeybees fed diets containing 1,000 and 2,000 μg/g L-ascorbic acid reared significantly more bees to the sealed stage than bees fed diets with 500 μg/g ascorbic acid or control bees. The levels of vitamin C in prepupae reared by bees ranged from 64.5 to 103.5 μg/g body mass. Vitamin C is either synthesized from simple precursors or from symbiotic microorganisms in the gut since honeybees fed the ascorbic acid-free control had equivalent levels of ascorbic acid to those fed the enriched diets. The total diet consumption by bees during the 10-week study showed that the four diets were equally attractive.
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    URL: http://dx.doi.org/10.1002/arch.940020104
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  • 18
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    Masthead (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985) 
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    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.940020201
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  • 19
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    Developmental pathology of Heliothis virescens larvae parasitized by Microplitis croceipes: Parasite-mediated host developmental arrest (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 131-143 
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    ISSN: 0739-4462
    Keywords: Heliothis virescens ; budworm ; Microplitis croceipes ; PTTH ; parasite ; host regulation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The developmental pathology of Heliothis virescens larvae parasitized by the braconid wasp Microplitis croceipes was examined. Parasitized host larvae begin the same precise sequence of developmental events in preparation for pupation as observed in unparasitized larvae. This sequence is initiated even though the host larval weight is below the normal developmental threshold for larval-pupal transformation. After parasite emergence, the host remains in a suspended advanced developmental state but never pupates. The developmental parameters altered by parasitization are normally under the host's endocrine control.Neck ligation of control larvae was used to identify the critical periods in parasitized and unparasitized fourth- and fifth-instar larvae. Control ligated fourth-instar larvae apparently released PTTH between 21:00 AZT of the second day of the instar and 1:00 AZT of the third day. Parasitized fourth-instar larvae were smaller and apparently released PTTH between 18:00 and 23:00 AZT of the third day. Control ligated fifth-instar larvae apparently released PTTH between day 1 and day 2 of the cell formation phase. Ligated fifth-instar parasitized larvae never molted to the pupal stage. Parasite larvae were adversely affected by host neck ligation with their pupal plus cocoon weight being proportional to the age of the host at the time of ligation.
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    Masthead (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985) 
    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.940020301
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    New ecdysteroid conjugate: Isolation and identification of 26-hydroxyecdysone 26-phosphate from eggs of the tobacco hornworm, Manduca sexta (L.) (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 227-236 
    Details
    ISSN: 0739-4462
    Keywords: 26-hydroxyecdysone 26-phosphate ; enzymatic hydrolysis ; ecdysteroid phosphate isolation ; ecdysteroid conjugate ; Manduca sexta ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The major ecdysteroid conjugate present in eggs (48-64 h old) of the tobacco hornworm has been purified by XAD-2 chromatography, C18 SEP-PAK separations, and ion suppression reversed-phase high-performance liquid chromatography. Enzymatic hydrolysis of the conjugate with acid phosphatase from human seminal fluid gave 26-hydroxyecdysone. The conjugate was identified as 26-hydroxyecdysone 26-phosphate by nuclear magnetic resonance and fast atom bombardment mass spectrometry. This compound is also the major conjugate of newly laid eggs (0-1 h old) of the tobacco hornworm. The role for ecdysteroid conjugates is discussed.
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    Sublethal effects of permethrin on the chemical communication system of the pink bollworm moth, Pectinophora gossypiella (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 283-293 
    Details
    ISSN: 0739-4462
    Keywords: Pectinophora gossypiella ; sublethal ; permethrin ; behavior ; communication ; pheromones ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Topically applied sublethal doses of permethrin can interrupt chemical communication between the sexes of Pectinophora gossypiella by affecting both the signaler and the responder. The probability of calling by females is reduced when they are treated with doses of permethrin which are much less than the LD50. Similarly, key stages in the behavioral response of males to sex pheromone are effectively blocked at these low doses. Males recover from these effects 4 days after treatment, but calling by females is still significantly reduced at this time. Chemical control of P. gossypiella populations with permethrin may not be limited to mortality, and potentially includes effective control of behavioral aspects of chemical communication.
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    Physiological investigation on the role of the innervation in the regulation of the prothoracic gland in Periplaneta americana (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 319-329 
    Details
    ISSN: 0739-4462
    Keywords: insect molt regulation ; prothoracic gland innervation ; nervous regulation of molt ; ecdysteroid release ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Under in vitro conditions the prothoracic gland nerve of the last larval instar of Periplaneta americana shows the same efferent nervous activity as under in situ conditions-ie, low activity at the 9th day and high activity at the 20th day of the molting interval. Isolation of the prothoracic ganglion from the subesophageal ganglion provokes an increase in this nerve activity, suggesting an inhibitory effect of the subesophageal ganglion on prothoracic gland nerve activity in vivo. Only in 20-day-old larvae does electrical stimulation of isolated prothoracic glands in vitro via the gland nerve result in a slightly increased release of ecdysteroids from the gland. This effect could not be influenced by different lengths of stimulation periods. Denervation of the prothoracic gland by transection of the gland nerve on the 13th day of the molting interval results in a complete abolition of the first peak of ecdysteroid production in the gland but has no influence on the occurrence and the amount of the main ecdysteroid peak just before the molt. The results suggest the participation of nervous activity in special periods of prothoracic gland regulation in the cockroach.
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    Isolation of an agent affecting the development of an internal parasitoid (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 375-384 
    Details
    ISSN: 0739-4462
    Keywords: host-parasitoid-baculovirus ; plasma-derived agent ; Pseudaletia unipuncta ; Glyptapanteles militaris ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The development of an internal braconid parasitoid, Glyptapanteles militaris, is adversely affected when its host, Pseudaletia unipuncta, is infected with the Hawaiian strain of granulosis virus. A plasma-derived agent, isolated from virus-infected hosts, was shown to elicit developmental aberrations in the parasitoid similar to those observed in virus-infected hosts. This agent was isolated by ammonium sulfate precipitation, gel filtration, and anion exchange chromatography, and its molecular weight, established by gel filtration and SDS-polyacrylamide gel electrophoresis, was determined to be about 64,000. The dilution end point of the agent and some stability properties were also established.
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    The role of the male accessory gland fluid in stimulating vitellogenesis in Aedes taeniorhynchus (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 405-413 
    Details
    ISSN: 0739-4462
    Keywords: Aedes taeniorhynchus ; male accessory gland fluid ; vitellogenesis ; microinjections ; EDNH ; fat body ; 20-OH-ecdysone ; tissue culture ; radioimmunoassay ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Injection of 20-hydroxyecdysone (20-OH-ecdysone) at high concentrations (5.0 μg) into intact or decapitated female Aedes taeniorhynchus induced vitellogenin synthesis, whereas low concentrations (5.0 ng) were ineffective. Injections of male accessory gland fluid (MAGF), however, at a concentration that was equivalent to 0.25 of the content of a pair of accessory glands, into intact or decapitated A. taeniorhynchus induced viteliogenin synthesis only in intact females. Ovariectomized mosquitoes did not synthesize vitellogenin after MAGF injection or blood feeding. Females that were first injected with MAGF and decapitated 12 h later synthesized viteliogenin at a rate that was 80% of intact controls.Egg development neurosecretory hormone (EDNH) activity in the heads of ovariectomized or intact females injected with MAGF was 9.0 pmol/min/head and 2.5 pmol/min/head, respectively, indicating that MAGF does not stimulate the corpus cardiacum (CC) to release EDNH.Incubation of MAGF and EDNH with fat bodies failed to induce vitellogenin synthesis. These results indicate that in A. taeniorhynchus the MAGF induces the ovary to release corpus cardiacum stimulating factor, which then signals CC to release stored EDNH.
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    Masthead (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985) 
    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.940020101
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    Ecdysteroid titre and metabolism to novel apolar derivatives in adult female Boophilus microplus (Ixodidae) (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 39-54 
    Details
    ISSN: 0739-4462
    Keywords: ecdysteroids ; fatty acyl esters ; ticks ; Ixodidae ; Boophilus microplus ; h.p.l.c. ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The free ecdysteroid titre determined by radioimmunoassay in adult female Boophilus microplus showed a peak just prior to full engorgement and detachment of the ticks and decreased subsequently to a very low value. In contrast, the titre of polar ecdysteroid conjugates was very low. Ecdysone was the major ecdysteroid at peak titre and was accompanied by much lower levels of 20-hydroxyecdysone. In newly detached ticks, injected [3H]ecdysone was metabolized primarily (80%) into much less polar compounds, which could be resolved into at least three groups by reversed-phase h.p.l.c. These [3H] “apolar” metabolites were transferred to the newly laid eggs, where they accounted for the vast preponderance of ecdysteroids, the level of free hormone being low. Hydrolysis of the three groups of compounds with an esterase preparation from porcine liver yielding [3H]ecdysone, together with the release of [3H] ecdysteroid and fatty acids upon alkaline saponification of the compounds, suggests that they are of a fatty acyl ester nature. The chemical transformation of these “esters” into the corresponding acetonide derivatives indicates that the 2- and 3-hydroxyls of ecdysone remain unsubstituted in these compounds. Several tick tissues, including Malpighian tubules, ovaries, gut, and fat body, metabolized [3H]ecdysone in vitro forming the “apolar esters” as major products. The maternal ecdysteroid “esters” may function as storage forms of hormone (presumably hormonally inactive), which could be hydrolysed enzymically during embryogenesis releasing free ecdysteroids. Such enzymic hydrolysis of [3H]ecdysone “esters” by homogenates from developing eggs of B. microplus has been demonstrated.
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    Juvenile hormone and 20-hydroxyecdysone as primary and secondary stimuli of vitellogenesis in Aedes aegypti (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 75-90 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Female Aedes aegypti that were fed blood and immediately abdominally ligated did not deposit yolk. Injection of 20-hydroxyecdysone (1.5-5.0 ng) or topical application of juvenile hormone (JH) analogue methoprene (25 pg) did not induce vitellogenesis in these abdomens. When blood-gorged ligated abdomens were treated with both hormones, however, vitellogenesis was stimulated in 60% of treated animals. Rocket immunoelectrophoresis indicated that vitellin concentration per follicle in treated animals was similar to that in intact controls. When ligated abdomens were first treated with methoprene and immediately injected with a crude head extract of egg development neurosecretory hormone, vitellogenin synthesis was induced at a rate similar to that in blood-fed controls. Methoprene at this concentration (25 pg), did not cause an increase in whole-body ecdysteroid titers. Larger amounts of methoprene (1.65 ng) were needed to stimulate egg development and ecdysteroid production.Implantation of ecdysone-secreting ovaries into ligated abdomens did not stimulate vitellogenesis in the recipients. However, in recipients that were first treated with methoprene (25 pg), implantation of ecdysone-secreting ovaries resulted in normal egg development.These experiments indicate that the appearance of JH precedes 20-hydroxyecdysone in stimulating vitellogenesis following blood feeding in Ae. aegypti.
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    N-acetylglucosaminyl transferases from the pupal instar of the stable fly, Stomoxys calcitrans (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 161-179 
    Details
    ISSN: 0739-4462
    Keywords: stable fly ; Stomoxys calcitrans ; N-acetylglucosaminyl transferases ; glycosyltransferases ; tunicamycin ; carbohydrate metabolism ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: N-acetylglucosaminyl transferases from pupae of Stomoxys calcitrans (L.) were studied in 10,000g pellet suspensions. Characterization of these enzymes was based on formation of glycolipids (ie, Dol·PP-GlcNAc and Dol·PP-(GlcNAc)2), oligosaccharide lipids, and giycoproteins. Studies on transferase activity during the pupal instar showed that there were two peaks of activity; the first peak was on day 0 (prepupae) and the second at 3 days after pupation. Subcellular fractionation indicated that 10,000g and 100,000g pellets contained most of the transferase activities. The transferases required divalent cations (either Mn2+ or Mg2+). The pH optimum, which varied for each of the products formed, was 7.5 for glycolipids, 7.0 for oligosaccharide lipids, and 6.5 for glycoprotein. Inclusion of dolichol monophosphate doubled the amount of Dol·PP-GlcNAc and Dol·PP·(GlcNAc)2 formed, but had little effect on oligosaccharide lipid and glycoprotein formation.Tunicamycin was a potent inhibitor of glycolipid formation with an I50 of 1.8-4.8 nM. It was confirmed that tunicamycin acts by preventing the transfer of GlcNAc-1-P from UDP-GlcNAc to Dol·P. UMP reverses glycolipid formation, yielding UDP-GlcNAc. Some characterization of the products was performed. Glycolipids were shown to be Dol·PP-GlcNAc and Dol·PP-(GlcNAc)2. Glycoprotein was rapidly solubilized by protease and detergent treatments, whereas oligosaccharide lipids appeared to be acid-labile, pyrophosphate-containing lipids. The apparent kinetic constants for the formation of glycolipids were as follows: UDP-GlcNAc Km = 1.55 ± 0.47 μM, Vmax = 0.66 ± 0.21 pmol·min-1·mg-1; Dol·P Km = 2.08 ± 0.85 μM, Vmax = 0.13 ± 0.06 pmol·min-1·mg-1 protein.
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    Effects of octopamine on fluid secretion by isolated salivary glands of a feeding ixodid tick (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 217-226 
    Details
    ISSN: 0739-4462
    Keywords: Amblyomma americanum ; dopamine ; octopamine ; salivary gland ; tick ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Octopamine elicited a dose-related secretory response by salivary glands isolated from the feeding female tick Amblyomma americanum. Half-maximal stimulation occurred at about 60 μM. Phentolamine (10 μM) failed to inhibit the octopamine-mediated response; however, thioridazine (50 μM) inhibited both octopamine (1,000 μM) and dopamine-stimulated (0.1 μM) secretion. Maximal stimulation by dopamine (1.0 μM) showed no further increase in the rate of secretion after adding octopamine (1,000 or 0.1 μM). Glands responded to octopamine (100 μM) with rates significantly lower than controls following exposure to amphetamine (1,000 μM). Octopamine receptors do not appear to mediate the secretory response, and octopamine may stimulate secretion by releasing catecholamines from presynaptic neurons. These results support the hypothesis that dopamine is the natural transmitter mediating fluid secretion in the feeding tick salivary gland.
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    Synthesis and deposition of chitin in larvae of the Australian sheep blowfly, Lucilia cuprina (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 251-263 
    Details
    ISSN: 0739-4462
    Keywords: Lucilia cuprina ; larval cuticle ; chitin synthesis ; chitin deposition ; chitin content ; larval growth ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Chitin synthesis in third-instar Lucilia cuprina larvae cultured at 23 °C was investigated using in vivo and in vitro systems, the latter with whole and with homogenized integuments. Synthesis was at a maximum between 24 and 48h after ecdysis from the second instar. Chitin was deposited in layers, and labeled GlcNAc was rapidly cleared from the hemolymph. In in vitro homogenate systems, the rapid conversion of UDP-([14C]GlcN)Ac to ([14C]GlcN)Ac and its 1-phosphate derivative contributed to the low incorporation of this precursor into chitin. The extent of the conversion was reduced by the addition of KCN or phenylthiourea. In in vivo and in vitro tissue systems the level of incorporation of ([14C]ClcN)Ac was higher than that of UDP-([14C]GlcN)Ac. However, in in vitro homogenate systems there was no difference unless UTP was added when the level of incorporation of only ([14C]GlcN)Ac was increased (by a factor of 9). Incorporation of UDP-([14C]GlcN)Ac, but not that of ([14C]GlcN)Ac, was decreased when larvae were deprived of food. Soluble oligosaccharides were detected in in vitro homogenate systems. They were formed during chitin synthesis and may represent newly initiated chitin chains. A reappraisal of current ideas on chitin synthesis in insects is needed.
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    Ecdysteroid receptors in a tumorous blood cell line of Drosophila melanogaster (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 295-317 
    Details
    ISSN: 0739-4462
    Keywords: ecdysteroids ; steroid hormone receptors ; Drosophila cell line ; haemocytes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The tumorous Drosophila melanogaster blood cell line BII has been studied for evidence for the presence of ecdysteroid receptors. The [3H]ponasterone A (pon A)* used in this study has been extensively purified, and the location of the tritium in the molecule has been partially determined. BII cells do not metabolise ecdysteroids. Intact cells demonstrate a considerable specific uptake of [3H]pon A which is saturable, apparently showing two specific components: a very high affinity component (KD = 0.3 nM) and a high affinity component (KD = 2 nM). The specific binding of [3H]pon A to whole cells is compatible with unlabelled ecdysteroids, but not with mammalian steroid hormones. The association rate constant (ka) for [3H]pon A was determined to be 3 × 107M-1min-1 at 21 °C, while the dissociation rate constant (kd) for the specifically bound [3H]pon A was found to be 4.4 × 10-3/min. Together, the kinetic rate constants yield a value of 0.15 nM for the KD.The receptors have been partially characterised in a cell-free extract prepared by sonification of the cells. The optimum pH for extraction and hormone binding is 8.2. Scatchard plots of binding data indicate that the cell-free extract also contains two high affinity specific binding components (kD = 0.1 nM and KD = 1 nM). The hgih affinity binders are macromolecular, as shown by chromatography on Sephadex G-25, and are susceptible to protease digestion, heat, and treatment with N-ethylmaleimide. Sucrose density centrifugation of the labelled receptor shows one peak at approximately 6S. The stability of the receptor preparation has been studied and conditions have been empirically determined (10% w/v sucrose, 25 mM dithioerthreitol, and 10 mM citrate), whereby the binding capacity of the unlabelled receptor is stable for at least 8 weeks if frozen at -20°C.
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    Characterization of juvenile hormone-binding proteins of hemolymph of Locusta migratoria (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 351-365 
    Details
    ISSN: 0739-4462
    Keywords: Locusta migratoria ; hemolymph ; juvenile hormone ; JH carrier protein ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The binding of juvenile hormone (JH) by components from hemolymph of adult female Locusta migratoria was characterized to establish whether hemolymph JH-binding proteins could be distinguished from a protein of fat body (BP-1) that may be a JH receptor. Hemolymph was analyzed by the hydroxyapatite assay, gel separation chromatography, polyacrylamide gel electrophoresis, and density gradient centrifugation. Three fractions that bound JH were separated from whole hemolymph by DEAE cellulose column chromatography, and these differed from all three cytosol-binding components. The major hemolymph component (H-A) showed relatively stable binding of JH, a slight loss of binding capacity after delipidation, and a Kd for JH-I of 16 nM. The Kds for JH-l and JH-lll with unfractionated hemolymph were 26 and 42 nM respectively. The order of effectiveness of competitors for binding of [3H]JH-l was JH-lll 〉 JH-l ≫ methoprene 〉 hydroprene ≫ acids of methoprene and hydroprene. The data indicated that unlabeled JH-lll was bound more effectively than its radioactive counterpart. The sedimentation values determined by sucrose density gradient ultracentrifugation were 13-14 S for hemolymph, and the sedimentation value was not altered by the inclusion of 0.4 M KCl throughout the gradient. The data indicated that H-A resembled the specific JH carriers and differed from the putative receptor of fat body cytosol by several criteria.
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    Characterization of proteolytic enzymes of the midgut and excreta of the biting fly Stomoxys calcitrans (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 145-159 
    Details
    ISSN: 0739-4462
    Keywords: trypsin ; proteases ; fly trypsin inhibitor ; midgut ; Stomoxys calcitrans ; pH optima ; blood digestion ; TAME ; hide powder azure ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Proteolytic enzymes were characterized in the midgut and the excreta of the stable fly Stomoxys calcitrans (L) with proteins, synthetic substrates, and inhibitors. Inhibition studies suggested trypsinlike activity in sugar-fed fly midguts, whereas excreta and blood-fed fly guts exhibited other proteases.Trypsinlike activity in midguts removed 20 and 30 h after a blood meal increased from 20% to 50% of the total proteolytic enzymes present. Trypsinlike activity was inhibited with human sera, trypsin-specific inhibitors, and a protein isolated from the stable fly thorax. When human albumin and globulin fractions were incubated with trypsinlike enzymes isolated from the midgut and excreta, the albumin fraction was less inhibitory than the globulin fractions and was readily hydrolyzed by the proteolytic enzymes. These results may indicate that the proteolytic enzymes produce an abortive complex with the globulin fractions of the sera. Such a complex may explain the temporary inhibition of proteolysis by the blood meal.Soybean trypsin inhibitor fed to stable flies caused 50% inhibition in proteolytic activity in the midguts of sugar-fed stable flies and 25% inhibition in the midguts of blood-fed stable flies. Complete inhibition of proteolytic enzyme activity was achieved only in vitro.pH profiles of proteolytic enzyme activity isolated from the excreta of blood-fed stable flies indicated that several proteolytic enzymes were excreted.
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    The disappearance of injected prostaglandins from the circulation of adult female australian field crickets, Teleogryllus commodus (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 367-374 
    Details
    ISSN: 0739-4462
    Keywords: T. commodus ; prostaglandins ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: During the first 2 h following injection of 0.02 μCi of [14C]-prostaglandin E2 into the abdomen of adult virgin female crickets, T. commodus, the concentration of radioactivity in the circulating hemolymph decreases. The reduction is associated with the increase in radioactivity in the Malpighian tubule/hindgut complex, ovaries, fat body, and, to a much smaller extent, ventral nerve cord and flight muscles. The finding that most, but not all, of the radioactivity in the hindgut is located in the contents of the lumen suggests that a high proportion of prostaglandins circulating in the hemolymph of T. commodus is eliminated by the usual excretory pathway. We suggest that the differential uptake of label from the circulating hemolymph by various tissues may be related to possible physiological functions that remain to be discovered.
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    Electronic Resource
    Isolation and characterization of highly purified mosquito oostatic hormone (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 333-349 
    Details
    ISSN: 0739-4462
    Keywords: Aedes aegypti ; Aedes taeniorhynchus ; column chromatography ; vitellogenesis ; oostatic hormone ; electrophoresis ; microinjections ; EDNH ; fat body ; tissue culture ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Oostatic hormone, the hormone that inhibits vitellogenesis in mosquitoes, was purified 7,000-fold with a recovery of 70% from the ovaries of the mosquito Aedes aegypti. The purification procedure included heat treatment and chromatography on ion exchange and gel filtration columns. The hormone is a small peptidelike molecule of molecular weight 2,200 at pH 4.5, which aggregates into larger molecular species of trimer and octamer at pH 7.0 as determined by gel filtration. The hormone is positively charged at pH 7.8 and has a low Rf at pH 9.4 on disc gel electrophoresis.Injection of purified oostatic hormone (9 ng) into female mosquitoes inhibited yolk deposition and vitellogenin synthesis. Activity of the oostatic hormone in the mosquito ovary increased rapidly following blood feeding and reached a maximum after 48 h. Oostatic hormone of A. aegypti injected into autogenous Aedes taeniorhynchus inhibited egg development. Repeated injections of dilute oostatic hormone at 24 h intervals partially arrested egg development, resulting in 60% reduction in the number of eggs laid. This hormone does not block release of egg development neurosecretory hormone (EDNH) from the mosquito brain but rather appears to act on the ovary.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020402
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    Electronic Resource
    Electronic Resource
    Ecdysone 20-monooxygenase in mitochondria and microsomes of Manduca sexta (L.) Midgut: Is the dual localization real? (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 2 (1985), S. 385-396 
    Details
    ISSN: 0739-4462
    Keywords: ecdysone 20-monooxygenase ; NADPH-cytochrome c reductase ; Manduca sexta ; tobacco hornworm ; midgut ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The dual localization of ecdysone 20-monooxygenase in mitochondria and microsomes of Manduca sexta larval midgut was investigated. Cosubstrate requirements and response to osmolarity of the microsomal ecdysone 20-monooxygenase system were found to be different from those previously reported for the mitochondrial enzyme system. The microsomal monooxygenase utilized NADPH and, less efficiently, NADH as cosubstrates. NADPH and NADH effects were neither additive nor synergistic. NADPH yielded identical activities in isotonic and hypotonic incubations. Mitochondria and microsomes showed no synergistic interaction for ecdysone 20-hydroxylation. After washing of the mitochondria, a large proportion of their ecdysone 20-monooxygenase activity was lost. The extent of the loss was inversely correlated to the concentration of mitochondria in the incubation mixture. The addition of bovine serum albumin to the incubations (2 mg/ml) largely restored the original activities. The microsomal contamination in mitochondrial pellets after each of three successive washings was determined by measuring the activity of a microsomal marker enzyme, NADPH-cytochrome c reductase. At each step of the purification, the ecdysone 20-monooxgenase activity of the mitochondrial preparations far exceeded the activity attributable to the microsomal contamination. These results confirm the existence of two independent ecdysone 20-monooxygenase systems in the midgut of M. sexta larvae.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020406
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