Allosteric behavior of platelet myosin

The allosteric properties of platelet actomyosin and myosin have been further studied. At pH 7.2, both exhibit sigmoid kinetics with at least two interacting ATP binding sites. At pH 8.9, the velocity versus substrate curve is shifted to the right and becomes more sigmoidal. In contrast, at pH 5.5, the enzyme appears to follow hyperbolic kinetics and the K m is reduced. In the presence of 1.4 m urea, the sigmoidicity is lost and the enzyme obeys Michaelis-Menten kinetics. The effect of ADP on the ATPase activity was also investigated. ADP shows characteristics of a competitive inhibitor; it increases K m (shifts sigmoid curve to the right) without affecting V. When the enzyme is desensitized by low pH (5.5) or urea (1.4 m), the allosteric interaction is abolished without impairing the catalytic activity and ADP is no longer inhibitory. These findings suggest that platelet myosin possesses two interacting sites and that ADP binds to the allosteric site which appears to be different from the catalytic site.