Clostripain
Clostripain (EC 3.4.22.8, 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]
References
- ↑ Mitchell, W.M. (1977). "Cleavage at arginine residues by clostripain". Methods Enzymol. 47: 165–170. doi:10.1016/0076-6879(77)47020-4. PMID 927173.
- ↑ Gilles, A.-M., Imhoff, J.-M. and Keil, B. (1979). "α-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain". J. Biol. Chem. 254: 1462–1468. PMID 762145.
- ↑ Gilles, A.-M., Lecroisey, A. and Keil, B. (1984). "Primary structure of α-clostripain light chain". Eur. J. Biochem. 145: 469–476. doi:10.1111/j.1432-1033.1984.tb08579.x. PMID 6391922.
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