A comparative study of heart myosin ATPase and light subunits from different species.

Heart myosin ATPase (measured with 10 mM CaCl2, and 0.60 M KCl) was found to be higher in rats (423 nmoles of Pi/min/mg) than in guinea-pig (268 nmoles of Pi/min/mg), dogs (139 nmoles of Pi/min/mg) or rabbits (94 nmoles of Pi/min/mg). Rat heart myosin ATPase was found to be higher than that from a pure red skeletal muscle myosin (soleus from guinea-pig: 286 nmoles/min/mg) and only one third lower than that from fast skeletal muscle myosin from rabbits. The heart myosin ATPase from rat, guinea-pig, and rabbit correlates with the maximum velocity of shortening at zero load of the myocardial muscle, as determined by other authors. These four cardiac muscle myosins have the same two light subunits (M.W.: 27000 and 18000) in SDS polyacrylamide gel electrophoresis; one of them (M.W.: 18000) exists in guinea-pig and dog as two different molecules having a different charge, as shown in urea electrophoresis, but in the rat, this subunit is also unique in urea gel electrophoresis. Rat heart, apparently, does not possess the phosphorylated light subunit (M.W.: 18,000) described by others in rabbit heart myosin. Attempts have been made to obtain a highly purified myosin, but this procedure does not suppress the striking difference which exists between rat and dog heart myosin ATPase.