Abstract
Studies of the isozymes produced by alternative alleles at the alcohol dehydrogenase locus of Drosophila melanogaster indicate that the ADH F enzyme is more active but less stable than the ADHS enzyme. The difference in stability is manifested in the responses to various conditions of temperature, pH, and protein concentration. The two enzymes also appear to differ in their substrate specificities. It is clear that the differences of primary structure involved in the ADH polymorphism can have profound effects on the biological activity of the molecule.
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This work was supported by the Nuffield Foundation and the Science Research Council.
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Day, T.H., Hillier, P.C. & Clarke, B. Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster . Biochem Genet 11, 141–153 (1974). https://doi.org/10.1007/BF00485770
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DOI: https://doi.org/10.1007/BF00485770