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A comparative study of enzyme activity variation between α-glycerophosphate and alcoholdehydrogenases in Drosophila melanogaster

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Abstract

An intraspecific comparison of α-glycerophosphate (α-GPDH: E.C.1.1.1.8) and alcohol dehydrogenase (ADH: E.C.1.1.1.1) enzyme activity levels was carried out in Drosophila melanogaster. The results indicate that (1) α-GPDH is a relatively conservative and ADH a relatively variable enzyme system with regard to structurally determined activity variation but that (2) the conservative nature of α-GPDH activity variation does not extend to the intra-genotypic level. The results are consistent with the view that different kinds of selective pressures are being exerted on the enzyme's structural and modifier gene loci.

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Authors and Affiliations

  1. Department of Genetics, Iowa State University, 8, Curtiss Hall, 50011, Ames, Iowa, USA

    Patricia G. Wilson & John F. McDonald

  2. Program in Molecular, Cellular and Development Biology, Iowa State University, 50011, Ames, Iowa, USA

    Patricia G. Wilson & John F. McDonald

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  1. Patricia G. Wilson
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  2. John F. McDonald
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Wilson, P.G., McDonald, J.F. A comparative study of enzyme activity variation between α-glycerophosphate and alcoholdehydrogenases in Drosophila melanogaster. Genetica 55, 75–79 (1981). https://doi.org/10.1007/BF00134008

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  • DOI: https://doi.org/10.1007/BF00134008

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