The activation of staphylococcal free coagulase by plasma constituents and the hydrolysis of Nα-toluene-p-sulphonyl-l-arginine methyl ester (TAME) by activated coagulase

Publisher Website
Google Scholar
Abstract
From a study made of the interaction between staphylococcal-free coagulase and the activator found in human plasma it appears that coagulase is enzymically degraded by coagulase activator. The active clotting material produced is either the enzyme-substrate complex or a degradation product of coagulase. In 0,07 [image] Na2HPO4-KH2PO4 at 37[degree]C, activation of coagulase proceeds most rapidly at pH 6.8. Activated coagulase was shown to hydrolyze the synthetic substrate N[alpha]-toluene-p -sulfonyl-L-arginine methyl ester. Hydrolysis of N[alpha]-toluene-p-sulfonyl-L-arginine methyl ester occurs most rapidly at pH 8.5; a Michaelis constant, of 3.3 x 10-3 [image] was calculated. Concentrations of N[alpha]-toluene-p-sulphonyl-L- arginine methyl ester down to 10-4 [image] were shown to inhibit the clotting of human plasma by free coagulase.

This publication has 11 references indexed in Scilit: