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The size and chemical nature of the myosin molecule have been studied extensively in enzyme preparations obtained from skeletal muscle (1-7), but a paucity of data is available on cardiac myosin. Furthermore, different values for the molecular weight of cardiac myosin have been reported. Olson (8) reported a value of 223,000 for the molecular weight of cardiac myosin whereas Gergely and Kohler (9) presented evidence that myosin from cardiac muscle has a molecular weight of 500,000, which is similar to that obtained during the most recent observations on skeletal muscle myosin (4-7). It has been suggested that the cardiac myosin molecule is altered in cardiac failure to form a stable aggregate of the basic monomer and that abnormal myosin prevents the formation of normal cardiac actomyosin (8). On the contrary, considerable evidence has been adduced that actomyosin from the failing heart is normal (10). The present observations were undertaken to determine the molecular size and chemical nature of normal cardiac myosin and to compare these data with results obtained on cardiac myosin from dogs with chronic congestive heart failure.

CHEMICAL CHARACTERIZATION OF CARDIAC MYOSIN FROM NORMAL DOGS AND FROM DOGS WITH CHRONIC CONGESTIVE HEART FAILURE