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  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (363)
  • Wiley-Blackwell  (363)
  • Elsevier
  • Wiley
  • 1985-1989  (363)
Collection
Keywords
Publisher
  • Wiley-Blackwell  (363)
  • Elsevier
  • Wiley
Years
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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020103
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  • 2
    Electronic Resource
    Electronic Resource
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020107
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  • 3
    Electronic Resource
    Electronic Resource
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020202
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  • 4
    Electronic Resource
    Electronic Resource
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020206
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  • 5
    Electronic Resource
    Electronic Resource
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020208
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  • 6
    Electronic Resource
    Electronic Resource
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020305
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  • 7
    Electronic Resource
    Electronic Resource
    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
    Electronic Resource
    Electronic Resource
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940020409
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  • 9
    Electronic Resource
    Electronic Resource
    Superoxide dismutase in the housefly, Musca domestica (L.) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 31-43 
    Details
    ISSN: 0739-4462
    Keywords: superoxide dismutase ; housefly ; Musca domestica ; enzyme purification and characterization ; rose bengal ; singlet oxygen ; enzyme deactivation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Four superoxide dismutase (SOD) (E.C. 1.15.1.1) isozymes were present in whole tissue homogenates of Musca domestica when examined by polyacrylamide gel electrophoresis. One of the isozymes contained manganese, and the other three contained copper and zinc. All were observed in each of the body tagma (head, abdomen, and thorax) and at each developmental stage (egg to adult).The copper- and zinc-containing isozymes purified from newly emerged, adult M. domestica had a relative molecular weight of 34,800 as determined by gel filtration chromatography but consisted of two equal-size subunits of 16,000 as measured by sodium dodecylsulfate polyacrylamide gel electrophoresis. An isoelectric point between 4.8 and 5.1 was measured. Approximately 2 mol each of copper and zinc were present per dimer. The three copper, zinc isozymes were identified as charge variants. The amino acid composition of the enzyme was similar to that of copper, zinc-containing superoxide dismutases from other sources.Purified housefly copper, zinc superoxide dismutase was neither deactivated nor able to protect lactic dehydrogenase against deactivation in the presence of light and rose bengal, a known generator of singlet oxygen. The role of SOD in the phototoxic reaction involving rose bengal is discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030105
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  • 10
    Electronic Resource
    Electronic Resource
    Biosynthesis and distribution of ecdysone and 20-OH-ecdysone in Aedes aegypti (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 19-30 
    Details
    ISSN: 0739-4462
    Keywords: Aedes aegypti ; methoprene ; ecdysone ; 20-OH-ecdysone ; egg development neurosecretory hormone ; HPLC ; TLC ; vitellogenesis ; RIA ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The distribution and biosynthesis of ecdysone and 20-hydroxyecdysone (20-OH-ecdysone) was followed in sugar- and blood-fed female Aedes aegypti. In both sugar- and early blood-fed animals most of the ecdysteroid determined by radioimmunoassay was found outside the ovary. Twenty-four to 40 h after blood feeding, however, ecdysteroid was distributed between ovary and carcass in the ratio of 1:1.5. Ecdysteroid titer reached a plateau between 18 to 40 h after the blood meal and decreased thereafter. Analysis of the ecdysteroid titer using thin layer chromatography (TLC) and high performance liquid chromatography (HPLC) revealed that both 20-OH-ecdysone and ecdysone were synthesized after the blood meal. The ratio of 20-OH-ecdysone to ecdysone remained essentially constant and fluctuated in parallel throughout egg development. Chromatography of the early ecdysteroid peak (8 h after feeding) using TLC and HPLC indicated that although it cross-reacted with ecdysteroid antibodies, it did not have the same elution times as ecdysone and 20-OH-ecdysone and is, therefore, probably a precursor of these ecdysteroids. Injections of egg development neurosecretory hormone (EDNH) preparation purified to near homogeneity, into ligated abdomens, induced ecdysteroid synthesis only if the abdomens were first treated with methoprene (12.5 pg). Methoprene at this concentration did not stimulate ecdysteroid synthesis in these abdomens. When blood-fed females were treated with [4-14C] cholesterol and analyzed using TLC and HPLC procedures, both [14C]labeled ecdysone and [14C]labeled 20-OH-ecdysone were synthesized in the ratio of 1:1.5. This report is the first to show that both ecdysone and 20-OH-ecdysone are synthesized in vivo in female A. aegypti.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030104
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