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Heat stability variants of esterase-6 in Drosophila melanogaster

Abstract

IT has been widely recognised that electrophoretic mobility alone does not distinguish all allelic variants of enzymes that exist in natural populations1–4. Recent applications of various techniques, among them examination of the heat stability of allozymes, have revealed the existence of allelic variants among allozymes with identical electrophoretic mobility5–8. I report here the existence and frequencies of heat-stability variants of esterase-6 in populations of Drosophila melanogaster, as well as an electrophoretic variant whose mobility is altered by some other, probably linked, modifier locus.

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COCHRANE, B. Heat stability variants of esterase-6 in Drosophila melanogaster. Nature 263, 131–132 (1976). https://doi.org/10.1038/263131a0

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