Purification and properties of a fibrinolytic enzyme from Bacillus subtilis

Abstract A fibrinolytic enzyme obtained from B. subtilis was purified, using DEAE‐cellulose column chromatography, and gel filtration on Sephadex G‐100. The preparation was homogeneous as tested by gel filtration on Sephadex G‐200, and disc electrophoresis. The molecular weight of this enzyme was 29.400 estimated by gel filtration on Sephadex G‐100. The optimum pH for enzyme activity was 7.2. Copper ions significantly increased enzyme activity, while Zn++ and Mn++ caused marked inhibition.