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Isozyme variability in species of the genusDrosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenases inD. melanogaster

✍ Scribed by C. L. Vigue; F. M. Johnson

Publisher: Springer
Year: 1973
Tongue: English
Weight: 746 KB
Volume: 9
Category: Article
ISSN: 0006-2928
DOI: 10.1007/bf00485735

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✦ Synopsis

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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