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]
YouTube Encyclopedic
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Kevin Ahern's Complete Lecture Set on PROTEIN PURIFICATION (3rd in a Series)
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7. Kevin Ahern's Biochemistry - Protein Purification II
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#07 Biochemistry Protein Characterization Lecture for Kevin Ahern's BB 450/550
Transcription
See also
References
- ^ 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. PMID 927173.
- ^ 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. PMID 762145.
- ^ 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. PMID 6391922.
External links
- clostripain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.4.22.8
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This page was last edited on 1 September 2023, at 21:25