Abstract
The kinetic properties of natural actomyosin (myosin B) ATPase, isolated from adult male houseflies, were examined. The ATPase was inhibited by increasing concentrations of KCl. At low ionic strength, both substrate inhibition and product inhibition were observed. The optimal temperature for ATPase activity was 45°C. Magnesium ions were necessary to activate the ATPase, and the enzyme was inhibited by 2 m M EGTA. Therefore, it was concluded that housefly actomyosin ATPase is quite similar to that of other species. The principal unique property of the housefly preparation (as in other insects with asynchronous flight muscles) is that the ATPase is activated by lower concentrations of calcium than the actomyosin ATPase of other species.
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