Determination of Some Biochemical Features of Alcohol Dehydrogenase from Drosophila Melanogaster, D. Simulans, D. Virilis, D. Funebris, D. Immigrans and D. Lebanonensis. Comparison of Their Properties and Estimation of the Homology of the Adh Enzyme of Different Species
Abstract
The enzyme alcohol dehydrogenase (ADH) has been one of most intensely studied enzymes in Drosophila melanogaster (Vigue and Johnson, 1973; Clarke, 1975; Thatcher, 1980). The structural locus of this enzyme, Adh, is polymorphic in natural populations and the mechanisms of the maintenance of this polymorphism are relatively well understood in D. melanogaster. Now D. melanogaster in general lives in environments with a high alcohol content, e.g., in wine cellars or fermenting fruits. In this paper we describe the properties of alcohol dehydrogenase in Drosophila species living in differing environments. In addition to D. melanogaster, we have chosen to study D. virilis, D. funebris and D. lebanonensis which live in comparable high-alcohol environments (wine cellars and breweries etc.) and tolerate high alcohol concentrations. D. simulans and D. immigrans are also cosmopolitan species, but do not exhibit a good tolerance, and they are only seldom found in high-alcohol environments. We describe the amino acid composition, subunit molecular weight, pH optima, isoelectric points, specific activity, molar absorption coefficient, apparent kinetic constants and stability parameters for each species and try to correlate the findings to the presumably adaptive responses of these species.
Keywords
Amino Acid Composition Alcohol Dehydrogenase Amino Acid Analysis Molar Absorption Coefficient Drosophila SpeciesPreview
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