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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. melanogaster 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.

BIOCHEMICAL DIFFERENCES BETWEEN PRODUCTS OF THE Adh LOCUS IN DROSOPHILA