Further evidence of thermostability variation within electrophoretic mobility classes of enzymes |
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Authors: | Roger Milkman |
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Affiliation: | (1) Department of Zoology, The University of Iowa, Iowa City, Iowa |
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Abstract: | Two Drosophila melanogaster strains, each heterozygous for fast and slow alleles at the Adh locus, and each having balanced second chromosomes, were found to differ in the apparent thermostability of the slow allozyme. The two strains were crossed, and F1heterozygotes were separated on the basis of the origin of the slow allele. After electrophoresis, the cellulose acetate strips were treated 1 1/2 min at 35 C. The putatively more sensitive allozyme showed a strikingly greater response to heat. These findings further support the conclusion that electrophoretically cryptic allelic differences exist which are expressed in thermostability differences. Further application of this approach has revealed one similar sensitive slow allozyme and three cases of a relatively resistant fast ADH allozyme in wild-caught flies.This work was supported by NIH Grant GM18967-02-03. |
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Keywords: | allozymes thermostability alcohol dehydrogenase Drosophila melanogaster |
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