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  • ASTROPHYSICS  (32)
  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (14)
  • 1985-1989  (44)
  • 1970-1974  (2)
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Years
Year
  • 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.
    Additional Material: 6 Ill.
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  • 2
    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.
    Additional Material: 3 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. 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.
    Additional Material: 4 Ill.
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  • 4
    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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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 1-33 
    ISSN: 0739-4462
    Keywords: regulation ; polyunsaturated fatty acids ; waxes ; pheromones ; prostaglandins ; linoleic acid synthesis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The composition, metabolism, and significance of fatty acids in insect biology are addressed. Fatty acids enter a number of metabolic pathways not directly related to energy storage and production; the unifying theme is that the fatty acids are not only structurally altered in these pathways, but that the alterations carry them from one area of biological significance into another. This theme is developed by offering a perspective on fatty acids in insects and then reviewing three major areas: 1) fatty acid composition, 2) biosynthesis of fatty acids (including polyunsaturated fatty acids and characteristics of certain biosynthetic enzymes), and 3) the biological significance of fatty acids. This last section includes discussions of the biochemistry of waxes, pheromones, and prostaglandins and the roles of fatty acids as components of defensive secretions. Little is known at the biochemical level about the regulation of fatty acid metabolism, and it is suggested that work in this area represents another frontier in insect biochemistry.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 357-366 
    ISSN: 0739-4462
    Keywords: linoleic acid ; lipid metabolism ; metamorphosis ; orthoptera ; insect ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Incorporation of [1-14C] acetate into various phospholipid and triacylglycerol fatty acids showed cyclic fluctuations in fatty acid biosynthesis that were similar for all of the major fatty acids in both male and female house crickets, Acheta domesticus, during development. All three stadia showed low levels of biosynthesis near ecdysis followed by increased synthesis to a peak at midstadium. In the phospholipid fraction, the incorporation of newly synthesized saturated fatty acids, 16:0 and 18:0, predominated near ecdysis, while at midstadium linoleic acid was the most actively synthesized fatty acid. In the triacylglycerol fraction, 18:0 and 18:1 predominated throughout the entire stadium.In contrast to the large fluctuations in fatty acid biosynthesis, the fatty acid compositions of the phospholipid and triacylglycerol fractions did not change within a stadium. However, significant differences were demonstrated between the stages and were associated primarily with differences between nymphal and adult stadia. Males and females differed in the proportions of 16:0 and 18:2 incorporated into phospholipids with females showing a greater proportion of 18:2 and a corresponding smaller proportion of 16:0 than males. The greater proportion of linoleic acid in females and in adults in general compared to nymphs and the predominance of the incorporation of newly synthesized linoleic acid into the phospholipid fraction of all stadia are consistent with the importance of this fatty acid in a number of biological roles.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 4 (1987), S. 191-203 
    ISSN: 0739-4462
    Keywords: cyanoprotein ; high molecular weight proteins ; immunology ; migratory locust ; storage proteins ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A high-molecular-weight protein, Mr 500,000, has been isolated and characterized from the hemolymph of the migratory locust, Locusta migratoria. It is composed of six seemingly identical subunits of apparent Mr 78,000. It contains low concentrations of carbohydrate and lipid, but high percentages of aspartate and glutamate as well as high proportions of hydrophobic amino acid residues. An antiserum, developed against this purified hemolymph protein, does not react in the double-diffusion test or after immunoblotting with purified lipophorin or cyanoprotein, two other major proteins in locust hemolymph. The concentration of this larval specific protein in the hemolymph of Locusta was examined during the last larval instar and in adult males by quantitative rocket immunoelectrophoresis. Its concentration increases in the second half of the fifth instar, concommitant with an increase in total protein. The protein is detectable by immunological techniques in adults, although its concentration is very low at this stage.
    Additional Material: 7 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 11 (1989), S. 159-172 
    ISSN: 0739-4462
    Keywords: JH-binding protein ; hemolymph proteins ; apolipophorin I ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Whole hemolymph from the American cockroach, Periplaneta americana, efficiently binds juvenile hormone (JH) III and to a lesser extent JH-I and 10, 11-epoxyfarnesyl diazoacetate (EFDA). The dissociation constants for racemic JH-III and EFDA are 30 ± 2 nM and 1.0 μM, respectively. Isolated lipophorin also binds [3H]JH-III and to a lesser extent JH-I. Other proteins from the hemolymph do not bind JH-III. Binding of JH-III to lipophorin is enantioselective. The dissociation constant, measured with a 92% 10R and 8% 10S mixture, is 21 ± 2 nM. Each lipophorin molecule contains one specific binding site for JH-III. It is concluded that lipophorin is the JH-III-specific transport protein in the hemolymph of the American cockroach. By a combination of photoaffinity labelling and gradient electrophoresis with sodium dodecyl sulphate on polyacrylamide gel, we showed that the JH-III-specific binding site is probably located on apolipophorin I.
    Additional Material: 7 Ill.
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  • 9
    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.
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  • 10
    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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