18O-exchange reactions of smooth muscle myosin of calf intestine were studied. Smooth muscle myosin, similar to skeletal myosin, catalyses two types of 18O-exchange reactions--intermediate and direct. Only quantitative differences of the exchange intensity are observed. 18O-exchange dependence on bivalent cation and nucleotide nature is found. The comparison of 18O-exchange characteristics for myosins of smooth and skeletal muscles confirms the hypothesis on the similarity of molecular mechanisms of ATP hydrolysis by myosin from different muscle types.
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