Abstract
We have isolated and purified two parental homodimers and a unique heterodimer of acid phosphatase [coded by Acph-1 (1.05)(F) and Acph-1 (0.95)(S)] from isogenic homozygotes and heterozygotes of Drosophila malerkotliana. F and S produce qualitatively different allozymes and the two alleles are expressed equally within and across all three genotypes and F and S play an equal role in the epigenetics of dominance. Subunit interaction in the heterodimer over a wide range of H+ concentrations accounts for the epigenetics of dominance for enzyme activity.
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