Adenosinetriphosphatase Activity of Cardiac Myosin

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Abstract
Examination of the ATPase activities of rabbit cardiac, rabbit red skeletal and rabbit white skeletal muscle myosins has demonstrated the existence of two types of myosin. One type, characterized by the higher ATPase activity, is present in white skeletal muscle; the other is found in red skeletal and cardiac muscle. The differences between myosin preparations could not be attributed to varying degrees of actin contamination nor to changes occurring in the myosins during the preparative procedure. Chromatography of dog cardiac myosin on DEAE-cellulose showed a single component. No differences were observed between the cardiac myosins of the dog and rabbit. Activation of the ATPase activity of cardiac myosin by Ca++ was less than that of white skeletal myosin while the extent of inhibition by Mg++ was similar for both. The stoichiometry of the interaction with actin of both cardiac and white skeletal myosins was similar but actin caused less activation of the cardiac myosin ATPase. Cardiac and white skeletal actins showed no differences in their abilities to activate myosin ATPase activity, which is in accord with previously documented similarities in the structures of these actins. Comparison of the present findings with previously reported mechanical measurements made with intact muscles does not indicate that the intrinsic level of myosin ATPase activity determines the maximal tension developed during the active state. On the other hand, there may be a direct relationship between shortening velocity and myosin ATPase activity.