Skip to main content
Log in

Analysis of genetic variation affecting the relative activities of fast and slow ADH dimers in Drosophila melanogaster heterozygotes

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

When Adh F/Adh S heterozygote homogenates are stained after electrophoresis, considerable variation is observed in the activity ratio of the FF dimer to the SS dimer. Two Adh S strains showed a sharp, consistent difference when crossed to a common Adh F strain. Optical scanning and genetic analysis confirmed that this difference originates close to the Adh locus. Since the morphs varied concordantly in their activities on numerous alcohols, and since aging and heat-treatment experiments failed to reveal a stability difference, it is proposed that the difference is regulatory in nature, affecting ADH synthesis and primarily cis-acting. A survey of wild flies revealed additional variation in the FF/SS activity ratio. Further genetic analysis showed that the basis of this variation is not restricted to the second chromosome. Furthermore, modification of the activity ratio implies some degree of allelespecificity on the part of the modifiers.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Adamkewizc, C. L., and Milkman, R. (1972). A multiple sample homogenizer/applicator for cellulose acetate electrophoresis. Drosophila Inform. Serv. 45192.

    Google Scholar 

  • Bewley, G. C. (1978). Heat stability studies at the α-glycerophosphate dehydrogenase locus in population of Drosophila melanogaster. Biochem. Genet. 16769–775.

    Google Scholar 

  • Danford, N. D., and Beardmore, J. A. (1979). Biochemical properties of esterase 6 in Drosophila melanogaster. Biochem. Genet. 171.

    Google Scholar 

  • Day, T. H., Hillier, P. C., and Clarke, B. (1974a). Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster. Biochem. Genet. 11141.

    Google Scholar 

  • Day, T. H., Hillier, P. C., and Clarke, B. (1974b). The relative quantities and catalytic activities of enzymes produced by alleles at the alcohol dehydrogenase locus in Drosophila melanogaster. Biochem. Genet. 11155.

    Google Scholar 

  • Hewitt, N. E., Pipkin, S. B., Williams, N., and Chakrabartty, P. K. (1974). Variation in ADH activity in class I and class II strains of Drosophila. J. Hered. 65141.

    Google Scholar 

  • Lewis, N., and Gibson, J. (1978). Variation in amount of enzyme protein in natural populations. Biochem. Genet. 16159.

    Google Scholar 

  • Lindsley, D. L., and Grell, E. H. (1967). Genetic Variations of Drosophila melanogaster, Carnegie Institute of Washington, Washington, D.C.

    Google Scholar 

  • Milkman, R. (1970). The genetic basis of natural variation. X. Recurrence of cve polygenes in natural populations of Drosophila melanogaster. Genetics 65289.

    Google Scholar 

  • Prakash, S. (1977). Allelic variants at the xanthine dehydrogenase locus affecting enzyme activity in Drosophila pseudoobscura. Genetics 87159.

    Google Scholar 

  • Sampsell, B. (1977). Isolation and genetic characterization of alcohol dehydrogenase thermostability variants occurring in natural populations of Drosophila melanogaster. Biochem. Genet. 15971.

    Google Scholar 

  • Singh, R. S., Lewontin, R. C., and Felton, A. A. (1976). Genetic heterogeneity electrophoretic “alleles” of xanthine dehydrogenase in Drosophila pseudoobscura. Genetics 84609.

    Google Scholar 

  • Thatcher, D. R. (1977). Enzyme instability and proteolysis during the purification of an alcohol dehydrogenase from Drosophila melanogaster. Biochem. J. 163317.

    Google Scholar 

  • Thompson, J. N., Jr., and Kaiser, T. N. (1977). Selection acting upon slow-migrating Adh alleles differing in enzyme activity. Heredity 38191.

    Google Scholar 

  • Thompson, J. N., Jr., Ashburner, M., and Woodruff, R. C. (1977). Presumptive control mutation for alcohol dehydrogenase in Drosophila melanogaster. Nature 270363.

    Google Scholar 

  • Ward, R. D. (1974). Alcohol dehydrogenase in Drosophila melanogaster: Activity variability in natural populations. Biochem. Genet. 12443.

    Google Scholar 

  • Ward, R. D., and Herbert, P. D. N. (1972). Variability of ADH activity in natural populations of D. melanogaster. Nature New Biol. 236243.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

This work was supported in part by money collected by Jewish Community of Iowa City, Iowa, and by NSF Grant 76-01903 to Roger Milkman.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Grossman, A. Analysis of genetic variation affecting the relative activities of fast and slow ADH dimers in Drosophila melanogaster heterozygotes. Biochem Genet 18, 765–780 (1980). https://doi.org/10.1007/BF00484592

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00484592

Key words

Navigation