Abstract
A chem.-mechanical theory of muscle contrac-tion is presented in which the contraction phase of myosin activity is considered to be the result of the condensation of the sulfhydryl and the phosphorylated hydroxyamino acid side-chains of the myosin molecule with the release of in-organic phosphate and formation of a thio-ether linkage. This could shorten the myosin molecule. Myosin relaxation would involve phosphorylytic cleavage of the thio-ether linkage by adenosine triphosphate to produce free sulfhydryl and phosphorylated hydroxyamino acid side-chains. The evidence is indirect and rests upon observations on the mechanism of conversion of homocysteine to cysteine by liver tissue of rats.

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