Clostripain (EC3.4.22.8, clostridiopeptidase B, clostridium histolyticum proteinase B, alpha-clostridipain, clostridiopeptidase, Endoproteinase Arg-C) is a proteinase that cleaves proteins on the carboxyl peptide bond of arginine.[1][2] It was isolated from Clostridium histolyticum. The isoelectric point of the enzyme is 4.8-4.9 (at 8 °C), and optimum pH is 7.4~7.8 (against α-benzoyl-arginine ethyl ester). The composition of the enzyme is indicated to be of two chains of relative molecular mass 45,000 and 12,500.[3]
^Gilles AM, Imhoff JM, Keil B (March 1979). "alpha-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain". The Journal of Biological Chemistry. 254 (5): 1462–8. PMID762145.
