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. 1977 Oct;87(2):285–304. doi: 10.1093/genetics/87.2.285

Genic Heterogeneity at Two Alcohol Dehydrogenase Loci in DROSOPHILA PSEUDOOBSCURA and DROSOPHILA PERSIMILIS

Jerry A Coyne 1, Alexander A Felton 1
PMCID: PMC1213741  PMID: 17248763

Abstract

A sequential electrophoretic survey of the second chromosome loci, alcohol dehydrogenase-6 (Adh-6) and octanol dehydrogenase ( Odh), was performed on 147 isochromosomal lines of Drosophila pseudoobscura and 60 lines of its sibling species, D. persimilis. Gels run with a variety of acrylamide concentrations and buffer pH's revealed the presence of 18 alleles of Adh-6 in the two species, where only eight had been previously detected by conventional electrophoretic methods. Only two alleles were added with our techniques to the previous total of nine in both species at the largely monomorphic Odh locus. Both enzymes show a predominance of one allele, with the other variants being fairly rare. There was no evidence of increased genetic divergence between the two species, but we found a striking increase in differentiation of Adh-6 alleles between the main body of D. pseudoobscura populations and the conspecific isolate from Bogotá, Colombia. These results are compared with our previous surveys of xanthine dehydrogenase in these species and discussed in reference to theories of genic polymorphism.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bernstein S. C., Throckmorton L. H., Hubby J. L. Still more genetic variability in natural populations. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3928–3931. doi: 10.1073/pnas.70.12.3928. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cochrane B. J. Heat stability variants of esterase-6 in Drosophila melanogaster. Nature. 1976 Sep 9;263(5573):131–132. doi: 10.1038/263131a0. [DOI] [PubMed] [Google Scholar]
  3. Coyne J. A. Lack of genic similarity between two sibling species of drosophila as revealed by varied techniques. Genetics. 1976 Nov;84(3):593–607. doi: 10.1093/genetics/84.3.593. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Johnson G. B. Hidden alleles at the alpha-glycerophosphate dehydrogenase locus in Colias butterflies. Genetics. 1976 May;83(1):149–167. doi: 10.1093/genetics/83.1.149. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Milkman R. Electrophoretic variation in Escherichia coli from natural sources. Science. 1973 Dec 7;182(4116):1024–1026. doi: 10.1126/science.182.4116.1024. [DOI] [PubMed] [Google Scholar]
  6. O'Brien S. J. Comparative analysis of malate dehydrogenases of Drosophila melanogaster. Biochem Genet. 1973 Oct;10(2):191–205. doi: 10.1007/BF00485765. [DOI] [PubMed] [Google Scholar]
  7. Ohta T. Role of very slightly deleterious mutations in molecular evolution and polymorphism. Theor Popul Biol. 1976 Dec;10(3):254–275. doi: 10.1016/0040-5809(76)90019-8. [DOI] [PubMed] [Google Scholar]
  8. Sieber F., Fox D. J., Ursprung H. Properties of octanol dehydrogenase from Drosophila. FEBS Lett. 1972 Oct 1;26(1):274–276. doi: 10.1016/0014-5793(72)80591-x. [DOI] [PubMed] [Google Scholar]
  9. Singh R. S., Hubby J. L., Lewontin R. C. Molecular heterosis for heat-sensitive enzyme alleles. Proc Natl Acad Sci U S A. 1974 May;71(5):1808–1810. doi: 10.1073/pnas.71.5.1808. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Singh R. S., Hubby J. L., Throckmorton L. H. The study of genic variation by electrophoretic and heat denaturation techniques at the octanol dehydrogenase locus in members of the Drosophila virilis group. Genetics. 1975 Jul;(3):637–650. doi: 10.1093/genetics/80.3.637. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Singh R. S. Substrate-specific enzyme variation in natural populations of Drosophila pseudoobscura. Genetics. 1976 Mar 25;82(3):507–526. doi: 10.1093/genetics/82.3.507. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Yutani K., Ogasahara K., Sugino Y., Matsushiro A. Effect of a single amino acid substitution on stability of conformation of a protein. Nature. 1977 May 19;267(5608):274–275. doi: 10.1038/267274a0. [DOI] [PubMed] [Google Scholar]

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