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

Author:

Drummond Margaret C.1,Tager Morris1

Affiliation:

1. Department of Microbiology, Division of Basic Health Sciences, Emory University, Atlanta, Georgia

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference17 articles.

1. Action of thrombin in the clotting of fibrinogen;BAILEY K., F.;Nature,1951

2. BLOMBACK B. AND I. YAMASHINA. 1958. On the N-terminal amino acids in fibrinogen and fibrin. Arkiv kemi 12:299-319.

3. Studies in blood coagulation. V. The coagulation of blood by proteolytic enzymes (tryspin, papain);EAGLE H.;J. Gen. Physiol.,1937

4. Assay of plasma prothrombin with a synthetic substrate;GLUECK H. I.;Proc. Soc. Exptl. Biol. Med.,1954

5. The activation of staphylococcal free coagulase by plasma constituents and the hydrolysis of N-toluene-p-sulfonyl-L-arginine methyl ester (TAMe) by activated coagulase;HAUGHTON G.;Biochem. J.,1959

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