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  • 11
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 85 (1973), S. 317-326 
    ISSN: 1432-1351
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 1. No appreciable seasonal changes were noticed in the composition of lipids and fatty acids ofCepaea nemoralis, nor was any indication obtained for a significant depletion of lipids during hibernation. 2. On account of the composition of lipids in this species of snail, the principal function of the lipids is probably structural rather than storage. 3. Although the fatty acid composition of the herbivorous snail is quite different from that of plants, no dietary influence on the fatty acid composition of the animal was detectable. 4. The fatty acid composition of the lipids appears not to be determined by environmental conditions.
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  • 12
    Electronic Resource
    Electronic Resource
    Springer
    Marine biology 20 (1973), S. 291-296 
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The fatty acid composition of 9 different tissues and organs of the female horseshoe crab Xiphosura (Limulus) polyphemus — one of the very few recent representatives of the ancient arthropod class Merostomata — was investigated in reference to the distribution of fatty acids through the marine food web. Fatty acid spectra, in which polyunsaturated fatty acids are predominant, especially eicosapentaenoic acid (20:5 ω3), revealed features characteristic of marine lipids. However, rather large quantities of monoenoic fatty acids also occur in all organs. In the saturated fatty acid fractions, the high content of branched-chain components is worth noticing, particularly in the gills and the carapace (35%); in all probability, the high amount of the branched-chain fatty acids is associated with their protective function in surface lipids. Isoprenoid fatty acids such as pristanic and phytanic acid were absent.
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  • 13
    ISSN: 1573-6857
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Alcohol dehydrogenase (ADH) of Drosophila not only catalyzes the oxidation of ethanol to acetaldehyde, but additionally catalyzes the conversion of this highly toxic product into acetate. This mechanism is demonstrated by using three different methods. After electrophoresis the oxidation of acetaldehyde is shown in an NAD-dependent reaction revealing bands coinciding with the bands likewise produced by a conventional ADH staining procedure. In spectrophotometric measurements acetaldehyde is oxidized in an NAD-dependent reaction. This activity is effectively inhibited by pyrazole, as specific inhibitor of ADH. By means of gas chromatographic analysis a quick generation of acetate from ethanol could be demonstrated. Our conclusion is further supported by experimental results obtained with either purified ADHF enzyme or genotypes with or without ADH, aldehyde-oxidase, pyridoxal-oxidase and xanthine-dehydrogenase activity. These results are discussed in relation to ethanol tolerance in the living organism in particular with respect to differences found between ADH in Drosophila melanogaster and D. simulans, and in relation to the possible implications for the selective forces acting on ADH-polymorphism.
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  • 14
    ISSN: 1432-0878
    Keywords: Lipoprotein ; Muscle ; Extracellular space ; Cryosectioning ; Immunocytochemistry ; Locust (Locusta migratoria)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Locust lipoproteins (lipophorins) were localized by indirect immunofluorescence- and immunogold labelling in cryosections of dorsolongitudinal flight muscles. Immunolabelling was performed with monoclonal antibodies against apolipoprotein epitopes that are exposed at the surfaces of the lipophorin particles. Both at rest and during flight, lipophorins were located only in the wider spaces of the extracellular matrix, in the basement membranes of the individual muscle fibers and in the extracellular spaces that surround interfibrillar tracheoles. No internalization of lipophorins by the flight muscle cells was observed. Our results indicate that the unloading of lipophorins at the flight muscles is an extracellular event. Similarities with the vertebrate system of chylomicron and very-low-density lipoprotein degradation are discussed.
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