Tight binding of arterial myosin to skeletal F-actin.

A study of the K+-activated myosin ATPase activity, which was measured at high ionic strength in the absence of divalent cations, permitted estimates of the actin-myosin interaction under conditions where (i) myosin-myosin interactions were prevented, (ii) the actin-myosin interaction could be studied in the presence of ATP, and (iii) variation in myosin light chain phosphorylation did not alter smooth muscle myosin ATPase activity. A comparison of myosins isolated from swine carotid arteries and mixed (leg and back) rabbit skeletal muscle was conducted in the presence and absence of rabbit skeletal actin. It was found that (i) arterial myosin, like skeletal myosin, exhibited hyperbolic kinetics for ATP hydrolysis, (ii) specific ATPase activities were significantly higher for skeletal myosin, (iii) saturating concentrations of actin appear to totally inhibit the arterial myosin ATPase activity, but only partially inhibit skeletal myosin activity, (iv) the free actin concentration required for half-maximal inhibition was significantly lower for the arterial myosin ATPase activity than for the skeletal myosin activity; (v) unlike skeletal actomyosin, arterial actomyosin exhibits tight binding characteristics in the presence of ATP, (vi) the binding stoichiometry for arterial myosin to skeletal F-actin was 2 mol of actin monomer/mol of myosin. These observations reveal differences in the interaction of arterial and skeletal myosin with actin, and may in part, explain the high force-generating characteristics of arterial smooth muscle.