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

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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.

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Authors and Affiliations

  1. In partial fulfillment of a Master's Degree, Biology Department, State University of New York at Albany, USA

    Stephen Miller

  2. Department of Biology, State University of New York at Albany, Albany, New York

    Stephen Miller, Robert W. Pearcy & Edward Berger

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  1. Stephen Miller
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  2. Robert W. Pearcy
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  3. Edward Berger
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Additional information

This work was supported by NIH Grant No. 18910 to E.B. and NSF Grant No. BO 36311 grant to R.W.P.

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Miller, S., Pearcy, R.W. & Berger, E. Polymorphism at the α-glycerophosphate dehydrogenase locus in Drosophila melanogaster. I. Properties of adult allozymes. Biochem Genet 13, 175–188 (1975). https://doi.org/10.1007/BF00486013

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  • DOI: https://doi.org/10.1007/BF00486013

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