Biochemical properties of esterase 6 in Drosophila melanogaster.
Biochemical properties of esterase 6 in Drosophila melanogaster were investigated using partially purified preparations from three genotypes, 1/1, 1/2, and 2/2. The molecular weight of the enzyme is estimated to be about 90,000, and treatment with sodium dodecylsulfate cleaves the enzyme into four units with a molecular weight of about 22,000. The activity toward 28 naturally occurring esters was assayed and shown to vary considerably with substrate, the 1/1 preparation having in general higher activity than 1/2 and 2/2, which were very similar. Heat sensitivity, the effect of metal ions, and the effects of the presence or absence of an end product were also studied. The differences demonstrated between allozymes would allow considerable scope, under appropriate conditions, for differential selection to operate between genotypes.
D000818:Animals; D003433:Crosses, Genetic; D004331:Drosophila melanogaster / Q000235:genetics*; D004950:Esterases / Q000235:genetics / Q000378:metabolism*; D005838:Genotype; D006358:Hot Temperature; D008670:Metals / Q000494:pharmacology; D008970:Molecular Weight; D010446:Peptide Fragments / Q000378:metabolism; D013379:Substrate Specificity
D008670:Metals; D010446:Peptide Fragments; D004950:Esterases