Clostripain Explained

Clostripain
Ec Number:3.4.22.8
Cas Number:9028-00-6

Clostripain (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]

See also

Notes and References

  1. Book: Mitchell WM . Cleavage at arginine residues by clostripain . Methods in Enzymology . 47 . 165–70 . 1977 . 927173 . 10.1016/0076-6879(77)47020-4 .
  2. Gilles AM, Imhoff JM, Keil B . alpha-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain . The Journal of Biological Chemistry . 254 . 5 . 1462–8 . March 1979 . 762145 .
  3. Gilles AM, Lecroisey A, Keil B . Primary structure of alpha-clostripain light chain . European Journal of Biochemistry . 145 . 3 . 469–76 . December 1984 . 6391922 . 10.1111/j.1432-1033.1984.tb08579.x . free .

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