The free heavy chain of vertebrate skeletal myosin subfragment 1 exhibits the same ATPase activity as the native isozyme and possesses the actin binding domain.
Vertebrate skeletal fast-twitch muscle myosin subfragment 1 is comprised of a heavy polypeptide chain of 95,000 daltons and one alkali light chain of either 21,000 daltons (A1) or 16,500 daltons (A2). In the present study, the heavy chain of subfragment 1 has been separated from the alkali light chain under nondenaturing conditions resembling those in vivo. The heavy chain exhibits the same ATPase activity as myosin subfragment 1, indicating that the heavy chain alone contains the catalytic site for ATP hydrolysis and that the alkali light chains are nonessential for activity. The free heavy chain associates readily at 4 degrees C or 37 degrees C with free A1 or A2 to form the subfragment 1 isozymes SF1(A1) or SF1(A2) respectively. Actin activates the MgATPase activity of the heavy chain in the same manner as occurs with the native isozyme, indicating that the heavy chain possesses the actin binding domain.
Sivaramakrishnan et al. (Fri,) reported a other. Separation of heavy chain from alkali light chain vs. Native isozyme (myosin subfragment 1) was evaluated on ATPase activity and actin binding. The free heavy chain of vertebrate skeletal myosin subfragment 1 exhibits the same ATPase activity as the native isozyme and possesses the actin binding domain.