Summary
Russell’s viper venom (RVV) is capable of hydrolyzing TAME slowly. It is readily adsorbed by glass from weak solutions. The pH optimum for the hydrolysis was 8.7 to 9.0. Under the conditions specified, Km was found to be 1.05 × 10–2 M and Vmax was 0.62 μM per min. per mg RVV. On a weight basis, RVV has a greater clot-accelerating activity than trypsin but less TAME hydrolyzing activity. It is suggested that there is a correlation between the clot-accelerating action of RVV and the hydrolysis of specific arginyl peptide bonds.