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  • Animals  (20)
  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (14)
  • 1985-1989  (34)
  • 1970-1974
  • 1
    Electronic Resource
    Electronic Resource
    Lipophorin in the larval and adult stages of Musca domestica (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 6 (1987), S. 39-48 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940060105
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  • 2
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    Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-04-07
    Description: Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuipers, O P -- Thunnissen, M M -- de Geus, P -- Dijkstra, B W -- Drenth, J -- Verheij, H M -- de Haas, G H -- New York, N.Y. -- Science. 1989 Apr 7;244(4900):82-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Utrecht, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2704992" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Crystallography ; Enzyme Activation ; Kinetics ; Molecular Sequence Data ; Mutation ; Pancreas/enzymology ; Phospholipases/*metabolism ; Phospholipases A/genetics/*metabolism/physiology ; Phospholipases A2 ; *Protein Conformation ; Snake Venoms/analysis ; Structure-Activity Relationship ; Swine
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Amplification of an esterase gene is responsible for insecticide resistance in a California Culex mosquito (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: An esterase gene from the mosquito Culex quinquefasciatus that is responsible for resistance to a variety of organophosphorus (OP) insecticides was cloned in lambda gt11 phage. This gene was used to investigate the genetic mechanism of the high production of the esterase B1 it encodes in OP-resistant Culex quinquefasciatus Say (Tem-R strain) from California. Adults of the Tem-R strain were found to possess at least 250 times more copies of the gene than adults of a susceptible strain (S-Lab). The finding that selection by pesticides may result in the amplification of genes encoding detoxifying enzymes in whole, normally developed, reproducing insects emphasizes the biological importance of this mechanism and opens new areas of investigation in pesticide resistance management.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mouches, C -- Pasteur, N -- Berge, J B -- Hyrien, O -- Raymond, M -- de Saint Vincent, B R -- de Silvestri, M -- Georghiou, G P -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):778-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3755546" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Culex/drug effects/enzymology/*genetics ; DNA/analysis ; Drug Resistance ; Esterases/*genetics ; *Gene Amplification ; *Genes ; Insecticides/*pharmacology ; Nucleic Acid Hybridization ; *Organophosphorus Compounds
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Alignment of rat cardionatrin sequences with the preprocardionatrin sequence from complementary DNA (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-19
    Description: Mammalian atria contain peptides that promote the excretion of salt and water from the kidney. When rat atrial tissue is extracted under conditions known to inhibit proteolysis, four natriuretic peptides, cardionatrins I to IV, are consistently isolated. These peptides derive from a common precursor, preprocardionatrin, of 152 amino acids, whose sequence was determined by DNA sequencing of a complementary DNA clone. Amino acid sequencing located the start points of cardionatrins I, III, and IV in the overall sequence. Cardionatrin IV most closely resembles procardionatrin because it begins immediately after the signal sequence at residue 25. Cardionatrin III begins at residue 73, and cardionatrin I, sequenced previously, begins at residue 123. Compositional analysis indicated that each of these cardionatrins extends up to tyrosine at position 150 but lacks the terminal two arginine residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flynn, T G -- Davies, P L -- Kennedy, B P -- de Bold, M L -- de Bold, A J -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):323-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3157217" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Atrial Function ; Atrial Natriuretic Factor ; Base Sequence ; Chromatography, High Pressure Liquid ; DNA/*genetics ; Electrophoresis, Polyacrylamide Gel ; Molecular Sequence Data ; Muscle Proteins/*genetics/isolation & purification ; *Peptide Fragments ; Protein Precursors/*genetics/isolation & purification ; Rats
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
    Electronic Resource
    Electronic Resource
    Inhibition of hydrocarbon biosynthesis in the housefly by 2-Octadecynoate (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 75-86 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030109
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  • 6
    Electronic Resource
    Electronic Resource
    Yolk polypeptide processing in the fat body of Sarcophaga bullata (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 87-96 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030710
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  • 7
    Electronic Resource
    Electronic Resource
    Developmental changes in fatty acid biosynthesis and composition in the house cricket, Acheta domesticus (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 357-366 
    Details
    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.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940090409
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  • 8
    Electronic Resource
    Electronic Resource
    Molecular characteristics of lipophorin, the juvenile hormone-binding protein in the hemolymph of the Colorado potato beetle (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 5 (1987), S. 255-269 
    Details
    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.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940050405
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  • 9
    Electronic Resource
    Electronic Resource
    Fatty acids in insects: Composition, metabolism, and biological significance (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 9 (1988), S. 1-33 
    Details
    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.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940090102
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  • 10
    Electronic Resource
    Electronic Resource
    Isolation and characterization of a larval hemolymph protein in Locusta migratoria (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 4 (1987), S. 191-203 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940040305
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