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  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (14)
  • 1985-1989  (14)
  • 1970-1974
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 6 (1987), S. 39-48 
    ISSN: 0739-4462
    Keywords: housefly ; hemolymph proteins ; metamorphosis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The major Musca domestica hemolymph lipoprotein, lipophorin, was purified from larval and from adult animals. The housefly lipophorin is composed of two apoproteins, apolipophorin I (Mr ∽ 253,000) and apolipophorin II (Mr ∽ 85,000). The lipophorin contains about 3.9% carbohydrates and reacts positively with concanavalin A. The density of larval lipophorin is equal to 1.152 g/ml and of adult lipophorin to 1.106 g/ml. The amount of lipophorin per animal increases during the larval stage, is constant during pupal stage, and suffers a great reduction at the pharate adult stage. The amount of lipophorin remains stable during the whole first gonotrophic cycle of the housefly. Lipophorin is not detected in the eggs of this insect.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 245-255 
    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.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 75-86 
    ISSN: 0739-4462
    Keywords: hydrocarbon biosynthesis ; 2-octadecynoate ; housefly ; fatty acid synthetase ; fatty acid elongation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The elongation of [9,10-3H]oleoyl-CoA with malonyl-CoA to form 20, 22, and 24 carbon monounsaturated fatty acids was demonstrated in housefly microsomes by radio-GLC. These elongation reactions, which have been postulated to be involved in hydrocarbon biosynthesis, have not been previously demonstrated in insects. 2-Octadecynoate (18:1 Δ2=) inhibited the in vivo incorporation of [1-14C]acetate into both fatty acids and hydrocarbons in a dose-dependent manner. At doses of 10 μg per female housefly of the alkynoic acid, the incorporation of [1-14C]acetate into hydrocarbon was inhibited 93%, the incorporation of [9,10-3H]oleate into hydrocarbon was inhibited 64%, and the incorporation of [1-14C]acetate into total internal lipid was inhibited 65%. Partially purified FAS was inhibited 50% and 95% at 15 μM and 40 μM, respectively, of the alkynoic acid. These results show that 2-octadecynoate inhibits hydrocarbon biosynthesis in the housefly by inhibiting FAS, and the in vivo data suggest that the elongation of 18:1 to longer chain fatty acids is also inhibited.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 87-96 
    ISSN: 0739-4462
    Keywords: yolk polypeptides ; 20-hydroxyecdysone ; in vitro translation ; processing ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In Sarcophaga bullata there are at least three genes coding for the major yolk polypeptides. By means of the reticulocyte cell-free translation system in combination with dog pancreatic microsomal membranes, it was demonstrated that minor processing of the peptides occurs in Sarcophaga. Prior to secretion, only the cleavage of the signal peptide is observed.In vitro translation experiments also revealed that Sarcophaga males require only 20-hydroxyecdysone and not juvenile hormone for the induction of the yolk polypeptide transcription. Following a single injection of 20-hydroxyecdysone in males, in vivo pulse labeling experiments showed that translation of the yolk polypeptides continues for no longer than 24-36 h; only a continuous stimulation by 20-hydroxyecdysone results in prolonged synthesis of the yolk polypeptides.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 5 (1987), S. 255-269 
    ISSN: 0739-4462
    Keywords: lipoproteins ; Leptinotarsa decemlineata ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Lipophorin, the protein that specifically binds juvenile hormone in the hemolymph of the Colorado potato beetle, Leptinotarsa decemlineata, is a high-density lipoprotein of Mr ∼ 574,000. Lipophorin contains 43% lipid and is composed of two apoproteins: apolipophorin I (Mr ∼ 251,000) and apolipophorin II (Mr ∼ 78,000). Both apoproteins contain mannose residues. Carotenoids make up a substantial part of the lipid fraction. Lipophorin constitutes about 25% of the total hemolymph proteins. Its concentration in the hemolymph (26 μM in 4-day-old long-day and 40 μM in 4-day-old short-day beetles) changes with different physiological conditions concomitant with changes in total protein content. Lipophorin specifically binds 10R-juvenile hormone III with high affinity. The dissociation constant for 10R-juvenile hormone III is 12 ± 2 nM. One lipophorin molecule contains one specific juvenile hormone-binding site. The concentration of binding sites therefore equals that of lipophorin in hemolymph.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 6 (1987), S. 227-265 
    ISSN: 0739-4462
    Keywords: hydrocarbon biosynthesis ; insect methylalkanes ; mass spectrometry of hydrocarbons ; development ; methodology ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The chemistry, biochemistry, and physiology of insect cuticular lipids are reviewed. The types of components present in cuticular extracts are described with special emphasis on the occurrence and identification of the di- and trimethylalkanes and the newly discovered tetramethylalkanes. The methods used in the extraction of cuticular components are discussed, including recommendations to standardize procedures. The structural elucidation of methylalkanes, particularly the mass spectral interpretation of multi-methyl-branched alkanes, is reviewed. The biosynthesis of cuticular lipids is discussed with emphasis on the hydrocarbon components, describing elongation reactions and the origin of the methyl branches. The effects of environment and development on cuticular lipids are reviewed.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 7 (1988), S. 105-118 
    ISSN: 0739-4462
    Keywords: JH binding ; lipoprotein ; migratory locust ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The juvenile hormone binding protein in Locusta migratoria is a very high density lipoprotein of Mr ∼ 566,000. It contains 15% lipid and is composed of six seemingly identical subunits of Mr ∼ 77,000. It is a minor protein, constituting 1-2% of the total hemolymph proteins. Its concentration fluctuates with total protein content and follows a cyclic pattern related to the molting cycles.The binding protein has a high affinity for (10R)-juvenile hormone III. The dissociation constant for the hormone is 3.7 ∼ 0.6 nM, and one binding molecule contains six hormone-specific binding sites. The concentration of binding sites in the hemolymph is therefore very high, reaching a value of 26 μM in the last larval instar and 11 μM in the adult male.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988), S. 127-134 
    ISSN: 0739-4462
    Keywords: Rhodnius prolixus ; precocious metamorphosis ; ecdysial stasis ; juvenile hormones ; precocene ; prothoracic glands ; regulation of ecdysone synthesis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Rhodnius prolixus nymphs fed 7-ethoxy-6-methoxy-2,2-dimethylchromene (ethoxyprecocene II, EPII) show a variety of responses, including precocious molting to diminutive adults, severe retardation of molting, or a condition of permanent ecdysial stasis. The latter two conditions are reversible by subsequent treatment with 20-hydroxyecdysone. Ecdysteroid titers in the hemolymph of individual insects, determined by radioimmunoassay (RIA), show that the ecdysteroid cycle in nymphs undergoing precocious metamorphosis is similar to that of untreated fifth stage nymphs during normal imaginal molting. Nymphs in ecdysial stasis, following EPII treatment, were found to have very low ecdysteroid titers. Analysis of ecdysteroid synthesis by the prothoracic glands (PG), cultured in vitro, showed that: 1) only traces of ecdysteroid were detectable in PG from nymphs treated in vivo with EPII; 2) the PG from untreated nymphs incubated in culture medium with EPII possessed significantly lower ecdysteroid synthesis compared with controls. These studies sought to determine if the inhibition of ecdysteroid biosynthesis observed in Rhodnius, following exposure to EPII in vivo and in vitro, is due to a direct action on the PG or result as an indirect effect perhaps mediated by the neuroendocrine system.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 193-203 
    ISSN: 0739-4462
    Keywords: Linoleic acid biosynthesis ; A. pisum ; polyunsaturated fatty acids ; symbiotes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The pea aphid Acyrthosiphon pisum (Harris) incorporated [1-14C]acetate into a phospholipid dienoic fatty acid in a time-dependent manner. In 2-h incubations, the incorporation of radioactivity into the 18:2 fraction was minimal, whereas after 45 h 18:2 was the major fatty acid labeled. Ozonolysis of the isolated dienoic fatty acid methyl ester followed by radio-gas-liquid chromatography showed that radioactivity was associated with fragments containing carbons 1-9 and 13-18. These data established the location of the double bonds in the 9,12 positions and indicated that the entire molecule was labeled from [1-14C]acetate. Tetracycline-treated aphids synthesized linoleic acid in the same proportions as untreated controls. Scanning electron microscopy showed that over 50% of the treated insects had greatly reduced numbers of intracellular symbiotes or lacked them or most of the existing symbiotes had an abnormal appearance. Therefore, we conclude that intracellular symbiotes are not involved in the biosynthesis of linoleic acid in the pea aphid.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 7 (1988), S. 133-143 
    ISSN: 0739-4462
    Keywords: Locusta migratoria ; juvenile hormone ; NCA-1 transection ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Exogenous farnesol or farnesoic acid (FA) stimulates juvenile hormone III (JH III) biosynthesis by isolated corpora allata from Locusta migratoria in a dose-dependent manner. Farnesol and FA also stimulate a dose-dependent accumulation of substantial amounts of methyl farnesoate (MF), identified by gas chromatography-mass spectroscopy (GCMS) analysis, in the corpora allata. Lower quantities of MF were found in the incubation medium. Corpora allata, denervated 2 days prior to assay, showed low spontaneous rates of JH biosynthesis which were stimulated by farnesol and FA. The dose-response curves for control and denervated corpora allata were similar. During oocyte maturation the rate of farnesol and FA stimulation of JH biosynthesis increased gradually. However, after transection of nervus corporis allati 1 (NCA-1), the rate of stimulated JH synthesis was maintained at preoperative levels. Although the spontaneous rate of JH biosynthesis decreased rapidly after NCA-1 transection, denervated glands could still be stimulated by farnesol or FA to produce large amounts of JH. These results suggest that the low spontaneous rate of JH biosynthesis in denervated corpora allata is not caused by inhibition of the final steps of JH biosynthesis.
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