Abstract
Blood-coagulating protease produced extracellularly by Cephalosporium sp. was purified. The purified enzyme moved homogeneously with a sedimentation constant, S20, W of 2.90 s by ultracentrifugation and gave a single protein band on the polyacrylamide gel electrophoresis. The enzyme was an EDTA-sensitive alkaline protease and Ca2+ stabilized its activity. Molecular weight of the enzyme was estimated as 39, 000 by Svedberg's method and 124, 000 by Andrews' method. The enzyme was considered to activate Factor X to Xa. The specific blood-coagulating activity of the enzyme was 1/5 of that of bovine thrombin.
