Biochemical Genetics

, Volume 13, Issue 3–4, pp 175–188 | Cite as

Polymorphism at the α-glycerophosphate dehydrogenase locus in Drosophila melanogaster. I. Properties of adult allozymes

  • Stephen Miller
  • Robert W. Pearcy
  • Edward Berger
Article

Abstract

A biochemical comparison was made between α-glycerophosphate dehydrogenase allozymes from Drosophila melanogaster. Enzymes extracted from the three major genotypes were indistinguishable in terms of their pH optima and thermal stabilities. Distinctive differences were observed for three parameters; temperature dependence of specific activity, temperature dependence of Km, and reaction rate constancy over a physiological temperature range. These results are discussed in terms of a model of balancing selection and the existence of spatial and temporal allele frequency clines in natural populations.

Key words

allozymes Drosophila populations Michaelis constant 

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Copyright information

© Plenum Publishing Corporation 1975

Authors and Affiliations

  • Stephen Miller
    • 1
    • 2
  • Robert W. Pearcy
    • 2
  • Edward Berger
    • 2
  1. 1.In partial fulfillment of a Master's Degree, Biology DepartmentState University of New York at AlbanyUSA
  2. 2.Department of BiologyState University of New York at AlbanyAlbany

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