Abstract
Adult Drosophila melanogaster from naturally occurring populations in the Eastern United States were examined by gel electrophoresis for their alcohol dehydrogenase (ADH) phenotype. The ADH enzymes were partially purified and characterized. Frequencies of the controlling alleles, Adh 4 and Adh 6, were discovered to vary in a clinal pattern. Adh 6 reaches a maximum frequency of about 0.90 in the South and minimum of about 0.50 in the North. Partially purified enzymes from the three Adh genotypes varied according to specific activity, substrate specificity, and heat stability. A differential influence of pH was indicated. There was little variation in K m values for ethanol and DPN+ among the enzymes.
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This work was supported by AEC Contract No. AT-(40-1)-3980 and by PHS Research Grant No. GM 11546.
Paper No. 3880 of the Journal Series of the North Carolina Experiment Station, Raleigh, North Carolina. This work incorporates, in part, the thesis research of C. L. Vigue to be submitted in partial fulfillment of the Ph.D. requirements in Genetics.
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Vigue, C.L., Johnson, F.M. Isozyme variability in species of the genus Drosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenases in D. melanogaster . Biochem Genet 9, 213–227 (1973). https://doi.org/10.1007/BF00485735
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DOI: https://doi.org/10.1007/BF00485735