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Drosophila alcohol dehydrogenase activity in vitro and in vivo: Effects of acetone feeding

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Abstract

When adult Drosophila are placed on medium containing 0.5% acetone, their level of alcohol dehydrogenase activity drops rapidly. At the same time, the proportion of activity in the various electrophoretic forms of the enzyme shifts; most of the activity becomes localized in what is ordinarily a minor form of the enzyme. Moreover, the loss of enzyme activity occurs in vivo as well, as shown by sensitivity to ethanol poisoning, insensitivity to pentenol treatment, and inability to utilize ethanol as an energy source. These observations are discussed in light of a model advanced for the origin of the multiple forms of alcohol dehydrogenase in Drosophila.

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References

  • Briscoe, D. A., Robertson, A., and Malpica, J. M. (1975). Dominance at Adh locus in response of adult Drosophila melanogaster to environmental alcohol. Nature 255148.

    Google Scholar 

  • David, J. (1977). Signification d'un polymorphisme enzymatique: La déshydrogénase alcoolique chez Drosophila melanogaster. Ann. Biol. 16451.

    Google Scholar 

  • David, J., and Clavel, M. F. (1965). Interaction entre le génotype et le milieu d'élevage: Conséquences sur les caractérístiques du développement de la drosophile. Bull. Biol. Fr. Belg. 99369.

    Google Scholar 

  • David, J., Fouillet, P., and Arens, M. F. (1974). Comparaison de la sensibilité à l'alcool éthylique de six espéces de Drosophila du sous-groupe melanogaster. Arch. Zool. Exp. Genet. 115401.

    Google Scholar 

  • David, J., Bocquet, C., Arens, M. F., and Fouillet, P. (1976). Biological role of alcohol dehydrogenase in the tolerance of Drosophila melanogaster to aliphatic alcohols: Utilization of an ADH null mutant. Biochim. Genet. 14989.

    Google Scholar 

  • David, J., Bocquet, C., Van Herrewege, J., Fouillet, P., and Arens, M. F. (1978). Alcohol metabolism in Drosophila melanogaster: The most active aldehyde oxidase produced by the Aldox locus is useless. Biochem. Genet. 16203.

    Google Scholar 

  • Everse, J., Zoll, E. C., Kahan, L., and Kaplan, N. O. (1971). Addition products of diphosphopyridine nucleotides with substitutes of pyridine nucleotide-linked dehydrogenases. Bioorg. Chem. 1207.

    Google Scholar 

  • Johnson, F. M., and Burrows, P. M. (1976). Isozyme variability in species of the genus Drosophila. VIII. The alcohol dehydrogenase polymorphism in North Carolina populations of D. melanogaster. Biochem. Genet. 1447.

    Google Scholar 

  • Lindsley, D. L., and Grell, E. H. (1968), Genetic Variations of Drosophila melanogaster, Carnegie Institution of Washington Publications, Washington, D.C.

    Google Scholar 

  • McKenzie, J. A., and Parsons, P. A. (1974). Alcohol tolerance: An ecological parameter in the relative success of Drosophila melanogaster and Drosophila simulans. Oecologia 10373.

    Google Scholar 

  • O'Donnell, J., Mandel, H. C., Krauss, M., and Sofer, W. (1977). Genetic and cytogenetic analysis of the Adh region in Drosophila melanogaster. Genetics 86553.

    Google Scholar 

  • Poulik, M. D. (1957). Starch gel electrophoresis in a discontinuous system of buffers. Nature 1801477.

    Google Scholar 

  • Schwartz, M., and Sofer, W. (1976a). Alcohol dehydrogenase-negative mutants in Drosophila: Defects at the structural locus? Genetics 83125.

    Google Scholar 

  • Schwartz, M., and Sofer, W. (1976b). Dietary induced alterations in the distribution of the multiple form of alcohol dehydrogenase in Drosophila. Nature 263129.

    Google Scholar 

  • Schwartz, M., Gerace, L., O'Donnell, J., and Sofer, W. (1975). Drosophila alcohol dehydrogenase: Origin of the multiple forms. In Third International Conference on Isozymes, Vol. I, Academic Press, New York.

    Google Scholar 

  • Sofer, W., and Hatkoff, M. A. (1972). Chemical selection of alcohol dehydrogenase negative mutants in Drosophila. Genetics 72545.

    Google Scholar 

  • Ursprung, H., and Leone, J. (1965). Alcohol dehydrogenase: A polymorphism in Drosophila melanogaster. Wilhelm Roux Arch. 164201.

    Google Scholar 

  • Van Herrewege, J., and David, J. (1974). Utilisation de l'alcool éthylique dans le métabolisme énergetique d'un insecte: Influence sue la duré de survie des adultes de Drosophila melanogaster. Compt. Rend. Acad. Sci. Paris 279335.

    Google Scholar 

  • Vigue, C. L., and Johnson, F. M. (1973). Isozyme variability in species of the genus Drosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenases in D. melanogaster. Biochem. Genet. 9213.

    Google Scholar 

  • Vigue, C. L., and Sofer, W. (1976). Chemical selection of mutants affecting alcohol dehydrogenase in Drosophila. III. Effects of ethanol. Biochem. Genet. 14127.

    Google Scholar 

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This research was supported by NIH Grants GM-18254 and ES-1527 and by DOE Contract No. EY-76-5-02-2965. Publication No. 1016 from the Department of Biology, Johns Hopkins University.

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Papel, I., Henderson, M., Van Herrewege, J. et al. Drosophila alcohol dehydrogenase activity in vitro and in vivo: Effects of acetone feeding. Biochem Genet 17, 553–563 (1979). https://doi.org/10.1007/BF00498890

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  • DOI: https://doi.org/10.1007/BF00498890

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