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Alcohol-oxidizing enzymes in 13 Drosophila species

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Abstract

Starch and polyacrylamide gel electrophoresis were used to ascertain the substrate specificities of alcohol-oxidizing enzymes in 13 Drosophila species. The substrates used were a variety of long- and short-chain aliphatic alcohols, one aromatic alcohol, and benzaldehyde. Only one enzyme (product of a single-gene locus) showed significant NAD+-dependent alcohol dehydrogenase activity with short-chain aliphatic alcohols. The 13 species, belonging to four different Drosophila groups, all showed a similar complement of alcohol-oxidizing enzymes, although differences in electrophoretic mobility and in levels of activity existed from species to species. These findings are relevant to the adaptation of Drosophila to alcohol environments.

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Author notes

  1. John F. McDonald

    Present address: Department of Genetics, Iowa State University, 50010, Ames, Iowa

Authors and Affiliations

  1. Department of Genetics, University of California, 95616, Davis, California

    Geoffrey K. Chambers, John F. McDonald, Michael McElfresh & Francisco J. Ayala

Authors
  1. Geoffrey K. Chambers
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  2. John F. McDonald
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  3. Michael McElfresh
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  4. Francisco J. Ayala
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Additional information

This study was supported by NIH Grant 1 PO1 GM 22221 and by Contract PA 200-14 Mod #4 with ERDA.

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Chambers, G.K., McDonald, J.F., McElfresh, M. et al. Alcohol-oxidizing enzymes in 13 Drosophila species. Biochem Genet 16, 757–767 (1978). https://doi.org/10.1007/BF00484733

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  • DOI: https://doi.org/10.1007/BF00484733

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