ENZYMATIC ACTIVITY OF STAPHYLOCOAGULASE II

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Abstract
Highly purified preparations of staphylocoagulase were shown to possess esterase activity in addition to the plasma-clotting activity. The differential effects of heat, trypsin, certain enzyme inhibitors, and antiserum fractions indicated the dual nature of these 2 activities. The tributyrinase was found to be more heat-labile than the clotting activity, being inactivated to a greater extent at 37 and 56[degree]C, the 2 temperatures studied. Concentrations of trypsin which totally eliminate the clotting activity reduce the tributyrinase only 43%. Concentrations of [gamma] -globulin-containing antiserum fractions which completely neutralize the clotting activity inhibit the tributyrinase only 66%. Of the enzyme inhibitors studied, both atoxyl and tetraethylpyrophosphate inhibit the clotting activity only, whereas NaF inhibits the tributyrinase while stimulating the plasma clotting. A physical separation of tributyrinase and the clotting principle was achieved by cellulose column zone electrophoresis.