ENZYMATIC ACTIVITIES ASSOCIATED WITH CLOTTING OF FIBRINOGEN BY STAPHYLOCOAGULASE AND COAGULASE-REACTING FACTOR AND THEIR INHIBITION BY DIISOPROPYLFLUOROPHOSPHATE

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Abstract
Drummond, Margaret C. (Emory University, Atlanta, Ga.) and Morris Tager. Enzymatic activities associated with clotting of fibrinogen by staphylocoagulase and coagulase-reacting factor and their inhibition by diisopropylfluorophosphate. J. Bacteriol. 83:975–980. 1962.—The chemical mechanism of fibrinogen clotting by staphylocoagulase and its plasma factor (CRF) involves a preliminary stage of proteolysis, analogous to that found in thrombin-catalyzed fibrinogen clotting. Coagulase-CRF also exhibits N-α-toluene-p-sulfonyl-l-arginine methyl esterase activity in addition to its fibrinogen-clotting and proteolytic activities. These enzymatic activities have been further studied by their responses to certain enzyme inhibitors, and from the standpoint of their possible interrelationships.