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

AUTOR(ES)

Drummond, Margaret C.

RESUMO

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.

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