Enzymatic Activities Associated With Clotting of Fibrinogen by Staphylocoagulase and Coagulase-Reacting Factor and Their Inhibition by Diisopropylfluorophosphate

Abstract

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-a-toluene-p-sulfonyl-L-arginine methyl ester

Staphylocoagulase *

“…Although we had found that coagulase alone failed to hydrolyze TAMe, it was reported that coagulase plus CRF, like thrombin, hydrolyzed TAMe (Haughton & Duthie, 1959). This observation was fully confirmed in our laboratory, although some differences were noted from the results of the British investigators when the reaction was studied in greater detail (Drummond & Tager, 19626). Thus, while the CRF used by Haughton and Duthie alone had no activity on TAMe, our CRF preparations all possessed this property, although significantly less than the combined effect of coagulase plus CRF.…”

“…Other similarities between thrombin and the coagulase-CRF complex soon became evident. It was found, for example, that both reactions are inhibited by diisopropylfluorophosphate (DFP), while neither is blocked by soybean trypsin inhibitor (Drummond & Tager, 19626).…”

Significance of Staphylocoagulase in Food Microbiology: A Review

“…Staphylocoagulase probably reacts with the CRF present i n plasma forming a complex which i n turn can act upon the fibrinogen. Drummond a n d Tager (1962) along with others (Haughton a n d Duthie 1959; Scheraga a n d Laskowski 1957; Zajdel et al. 1973), reported t h a t the action of the coagulase-CRF complex upon fibrinogen involved a preliminary stage of proteolysis similar to that caused by thrombin, a n enzyme responsible for physiological blood clotting.…”

“…Haughton a n d Duthie (1959) found that like thrombin, a n d certain other proteins with coagulating capabilities, coagulase-CRF complex possesses esterease activity on a synthetic substrate, N-2 toluene-psulfonyl-L-arginine methyl ester. Drummond a n d Tager (1963) noted t h a t when fibrinogen was converted into insoluble fibrin a n d fibrino peptides, the latter were released in a manner similar to the thrombin degradation of fibrinogen. They reported both types of fibrino peptides (from coagulase a n d thrombin) were physicochemically identical suggesting that coagulase-CRF complex resulted in thrombin formation.…”

Fibrinogen Clotting and Fibrino-Peptide Formation by Staphylocoagulase and the Coagulase-Reacting Factor

“…Like thrombin, and certain other proteins with coagulating capabilities, coagulase incubated with the plasma factor possesses esterase activity on a synthetic substrate, N-a-toluene-p-sulfonyl-L-arginine methyl ester (TAMe; Haughton and Duthie, 1959). Like thrombin, coagulase-CRF is inhibited in its fibrinogen-clotting and TAMe-esterase activities by diisopropylfluorophosphate but is unaffected by soybean trypsin inhibitor (Drummond and Tager, 1962b).…”