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Abstract The proteolytic enzyme, clostridiopeptidase B (clostripain), from Clostridium histolyticum culture filtrates has been purified to apparent homogeneity as judged by ultracentrifugation, electrophoresis in polyacrylamide gels, immunodiffusion, and immunoelectrophoresis. The enzyme has an apparent molecular weight of 50,000 from sedimentation equilibrium studies. Optical rotatory dispersion studies suggest a low α-helical content. Clostridiopeptidase B exhibits proteolytic as well as amidase-esterase properties. The specificity is confined primarily to arginine residues, although hydrolysis proceeds to a minor degree in most lysine-containing substrates.
Mitchell et al. (Sun,) studied this question.