Summary
A biochemical approach is utilised in the study of the maintenance of variation at the Adh locus in Drosophila melanogaster. There is a direct correlation between biochemical findings and the results of competition experiments. The relevance of these findings to the study of other enzyme polymorphisms is discussed.
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References
Clarke, B. 1970. Darwinian evolution of proteins. Science, 168, 1009–1011.
Day, T H, Hillier, P C, and Clarke, B C. 1974. Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster. Biochem Genet, 11, 141–153.
Gibson, J. 1970. Enzyme flexibility in Drosophila melanogaster. Nature, 227, 959–960.
Kalmus, H. 1943. A factorial experiment on the mineral requirements of a Drosophila culture. Amer Natur, 77, 376–380.
Kimura, M, and Ohta, T. 1971. Protein polymorphism as a phase of molecular evolution. Nature, 229, 467–469.
Kojima, K I, and Tobari, Y N. 1969. The patterns of viability changes associated with genotype frequency at the alcohol dehydrogenase locus in Drosophila melanogaster. Genetics, 61, 201–209.
Lewontin, R C, and Hubby, J L. 1966. A molecular approach to the study of genie heterozygosity in natural populations. II. Amount of variation and degree of heterozygosity in natural populations of Drosophila pseudoobscura. Genetics, 54, 595–609.
Manly, B F J. 1972. Tables for the analysis of a selective predation experiment. Res Popul Ecol, 14, 74–81.
Rasmuson, B, Nilson, L R, Rasmuson, M, and Zeppezauer, E. 1966. Effects of heterozygosity on alcohol dehydrogenase (ADH) activity in Drosophila melanogaster. Hereditas, 56, 313–316.
Richmond, R C. 1970. Non-Darwinian evolution: A critique. Nature, 225, 1025–1028.
Sofer, W H, and Hatkoff, M A. 1972. Chemical selection of alcohol dehydrogenase negative mutants in Drosophila. Genetics, 72, 545–549.
Tecwyn Williams, R. 1949. Detoxication Mechanisms. Chapman and Hall, London.
Vigue, C L, and Johnson, F M. 1973. Isozyme variability in species of the genus Drosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenase in D. melanogaster. Biochem Genet, 9, 213–227.
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Morgan, P. Selection acting directly on an enzyme polymorphism. Heredity 34, 124–127 (1975). https://doi.org/10.1038/hdy.1975.12
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DOI: https://doi.org/10.1038/hdy.1975.12
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