Clostripain
Clostripain(EC3.4.22.8,clostridiopeptidase B,clostridium histolyticum proteinase B,Alpha -clostridipain,clostridiopeptidase,Endoproteinase Arg-C) is aproteinasethat cleavesproteinson the carboxyl peptide bond ofarginine.[1][2]It was isolated fromClostridium histolyticum.Theisoelectric pointof theenzymeis 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 relativemolecular mass45,000 and 12,500.[3]
See also
[edit]References
[edit]- ^Mitchell WM (1977).Cleavage at arginine residues by clostripain.Methods in Enzymology. Vol. 47. pp. 165–70.doi:10.1016/0076-6879(77)47020-4.PMID927173.
- ^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.
- ^Gilles AM, Lecroisey A, Keil B (December 1984)."Primary structure of Alpha -clostripain light chain".European Journal of Biochemistry.145(3): 469–76.doi:10.1111/j.1432-1033.1984.tb08579.x.PMID6391922.
External links
[edit]- clostripainat the U.S. National Library of MedicineMedical Subject Headings(MeSH)
- EC3.4.22.8
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