Biochemical differences between products of the Adh locus in Drosophila

Mauro Santos, John F McDonald

Research output: Contribution to journalArticleResearchpeer-review

45 Citations (Scopus)

Abstract

An analysis of the molecular properties of the major alcohol dehydrogenase
(E.C.1.1.1.1) allozyme variants found segregating in natural populations of
D. mehnogaster is presented. Our results indicate: (1) ADH-S enzyme has
generally lower Michaelis-Menten constants than those of ADH-F; (2) ADH-S
and ADH-F enzymes display opposite interactions for both co-factor and substrate; and (3) higher levels of ADH are associated with the Adh-fast genotype.
The possible adaptive significance of these findings is discussed.
Original languageEnglish
Pages (from-to)1013-1022
Number of pages10
JournalGenetics
Volume95
Publication statusPublished - Aug 1980

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