Abstract
1. 1. Five partially purified allozymes of Esterase-5 (EST-5 0.85, EST-5 0.95, EST-5 1.00, EST-5 1.07–1.17, and EST-5 1.12) of Drosophila pseudoobscura did not differ with respect ot substrate specificity except for small differences in the presence of dimethylformamide. 2. 2. The most common allozyme (EST-5 1.00) was far more heat stable than the others. 3. 3. The two most common alloyzmes (EST-5 10.00 and EST-5 1.12) were more stable in urea than the others. 4. 4. Approximately half of the soluble esterase activity was EST-5.
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