[Alcohol dehydrogenase and adaptation to ethanol in Drosophila].
The subject of this research is activity and allozyme spectra of alcohol dehydrogenase (ADH), and survival of mutant strains of Drosophila kept in standard nutrient medium with added ethanol. In all experiments the ADH of flies revealed greater affinity to isopropanol than ethanol. The mutant strains considerably differed from one another and from the wild type of flies in the level of enzyme activity, which may be connected with genotypic properties in the mutants studied. The ADH variability in mutant strains seems to be caused by different alleles of the structural ADH gene, which was established as a result of investigation of activity, electrophoretic mobility and thermostability of corresponding allozymes. As follows from experiments on the genotypical structure of populations in the conditions of fly selection in the medium containing ethanol (10%), the adaptation of flies to exogenous ethanol takes place via mechanisms of allele control of the ADH activity. Phenotypical manifestation of the ADH locus and its effect on the resistance of Drosophila to alcohol are supposed to depend on complex gene interactions determined by the genotype as a whole.
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Totskiĭ
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D000222:Adaptation, Physiological / Q000235:genetics*; D000426:Alcohol Dehydrogenase / Q000235:genetics* / Q000378:metabolism; D000483:Alleles; D000818:Animals; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics* / Q000502:physiology; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D000431:Ethanol / Q000494:pharmacology*
D000431:Ethanol; D000426:Alcohol Dehydrogenase
Alkogol'degidrogenaza i adaptatsiia k étanolu u drozofily.