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  • 1
    Electronic Resource
    Electronic Resource
    Hepatic steatosis in artificially fed marine teleosts (1998)
    Oxford, UK : Blackwell Science Ltd
    Journal of fish diseases 21 (1998), S. 0 
    Details
    ISSN: 1365-2761
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In a comparison of livers in fish (Sparus auratus and Dicentrarchus labrax) feeding on natural sources of food with livers of artificially fed animals, a much higher C18:1/C22:6 ratio was observed in the latter. Staining livers with oil red O showed extensive steatosis in artificially fed fish, but not in those naturally fed. Juvenile artificially fed fish showed a more extensive steatosis and a higher mortality rate. In steatotic fish fed a natural diet for 2 months, the liver exhibited extensive regeneration and only a few steatotic areas remained. Marine teleosts do not appear to have a proliferative response of peroxisomes and this is likely to contribute to liver lipid accumulation and subsequent steatosis. It is suggested that an excess of C18:1 (or other mono-unsaturated fatty acids), coupled with a lack of adaptive peroxisomal proliferation, is the primary cause of lipid droplet formation leading to hepatic steatosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2761.1998.00089.x
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of phospholipase A2 on purified gastric vesicles (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 429-444 
    Details
    ISSN: 0091-7419
    Keywords: (H++K+)-ATPase ; transport ATPase ; proton transport ; phospholipids ; phospholipase A2 ; CD spectrum ; gastric ATPase ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The phospholipid and fatty acid composition and role of phospholipids in enzyme and transport function of gastric (H++K+)-ATPase vesicles was studied using phospholipase A2 (bee venom). The composition (%) was phosphatidylcholine (PC) 33%; sphingomyelin (sph) 25%; phosphatidylethanolamine (PE) 22%; phosphatidylserine (PS) 11%; and phosphatidylinositol (PI) 8%. The fatty acid composition showed a high degree of unsaturation. In both fresh and lyophilized preparations, even with prolonged incubation, only 50% of phospholipids were hydrolyzed, but the amount of PE and PS disappearing was increased following lyophilization. There was a marked decrease in K+-ATPase activity (75%) but essentially no loss of the associated K+ p-nitrophenyl phosphatase was found. ATPase activity could be largely restored by various phospholipids (PE 〉 PC 〉 PS). There was also an increase in Mg2+-ATPase activity, partially reversed in fresh preparations by the addition of phospholipids (PE 〉 PS 〉 PC). Proton transport activity of the preparation was rapidly inhibited, initially due to a large increase in the HC1 permeability of the preparation. Associated with these enzymatic and functional changes, the ATP-induced conformational changes, as indicated by circular dichroism spectra were inhibited.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400110402
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  • 3
    Electronic Resource
    Electronic Resource
    Conformation of bombesin in buffer and in the presence of lysolecithin micelles: Nmr, CD, and fluorescence studies (1989)
    New York : Wiley-Blackwell
    Biopolymers 28 (1989), S. 441-463 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformation of the tetradecapeptide hormone bombesin has been studied in buffer and in the presence of lysolecithin micelles, using static and dynamic fluorescence, CD, and one- and two-dimensional nmr. The results obtained show that in buffer bombesin is present in an extended flexible chain, with no evidence for any ordered secondary structure. A marked change in the CD spectrum is observed changing from buffer to the lipid suspension. Concomitantly, the 1H-nmr spectrum of bombesin, in a D2O lipid dispersion, shows the persistence of resonances due to exchangeable protons and in similar conditions the fluorescence intensity increases. We think therefore that these results strongly support the hypothesis that bombesin interacts with the lipid phase, assuming ordered secondary structure. Finally, the marked dependence of tryptophan fluorescence quantum efficiency and order parameter from the hormone concentration in the presence of lysolecithin but not in buffer leads to the conclusion that bombesin can associate into the lipid matrix.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360280140
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  • 4
    Electronic Resource
    Electronic Resource
    Fluorescence and CD studies on the conformation of the gastrin releasing peptide in solution and in the presence of model membranes (1991)
    New York : Wiley-Blackwell
    Biopolymers 31 (1991), S. 653-661 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformation of the heptacosapeptide hormone, gastrin releasing peptide, has been studied in buffer and in the presence of lipids, using static and dynamic fluorescence and CD. The results obtained show that, in buffer, the hormone exists in a collection of flexible, random coil type conformers, characterized by a β-turn between residues 14-19. On the other hand, organic solvents can induce some degree of ordered secondary structure in the peptide chain.The marked changes, observed in CD and fluorescence spectra upon addition of lysolecitin micelles and dimyristoylphosphatidylserine vesicles, clearly show that the peptide interacts with lipids, assuming a lipid specific configuration. Interestingly, no significative spectroscopic changes are produced by exposure to dimyristoylphosphatidylcholine vesicles both in the gel and liquid-chrystalline phases, suggesting a requirement for negatively charged lipids during the process of hormone-membrane interaction.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360310610
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