Genetics of esterases inDrosophila. IX. Characterization of the JH-esterase inD. virilis

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Abstract
The kinetic characteristics of the main isozymes ofDrosophila virilis esterase were studied andK m values of esterase-2, -4, and -6 and p-esterase for α- and β-naphthyl acetate were obtained. Juvenile hormone (JH) was shown to inhibit the p-esterase activity when in competition with β-naphthyl acetate and the general esterase inhibitor, diisopropylphosphofluoridate (DFP), was shown to inhibit all the components of theD. virilis esterase patterns except p-esterase. While studying the changes of p-esterase activity inD. virilis ontogenesis, the increase in p-esterase activity in the wandering larvae, prepupae, and early pupae was found to correlate with a decrease in JH titer at these stages. The decrease in JH level in a temperature-sensitive lethal mutant larvae ofD. virilis at high temperatures was shown to correlate with increased p-esterase activity. These results confirm that p-esterease ofD. virilis is JH-esterase.