Abstract
The denaturation process of actomyosin during storage in 0.6M KCl at pH 5.7 and 25°C was studied by measuring ATPase activity, turbidity and solubility. During the storage of actomyosin the inactivation rate of myosin A ATPase was similar to that of the ATPase activating ability of F-actin. While the inactivation rate of isolated Factin was largely dependent on the initial protein concentration, that of F-actin in actomyosin was less dependent. When F-actin was stored alone, inactivation of the ATPase activating ability was accompanied with a remarkable increase in turbidity and a decrease in solubility. However, this was not true when F-actin was stored with myosin A.
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