| Identification | Back Directory | [Name]
CLOSTRIPAIN | [CAS]
9028-00-6 | [Synonyms]
PROTEINASE
EC 3.4.22.8
CLOSTRIPAIN
IUB: 3.4.22.8
E.C. 3.4.4.20
alpha-Clostripain
ENDOPROTEINASE-ARG-C
CLOSTRIDIOPEPTIDASE B
clostripain from clost. histolyticum
Clostridium histolyticum proteinase B
Proteinase, Clostridium histolyticum, B
Proteinase from Clostridium histolyticum
CLOSTRIPAIN FROM CLOST. HISTOLYTICUM >1
Native Clostridium histolyticum Clostripain
Clostripain NB from Clostridium histolyticum
Endoproteinase Arg-C from Clostridium histolyticum
Clostridiopeptidase B, Proteinase from Clostridium histolyticum | [EINECS(EC#)]
232-822-2 | [MDL Number]
MFCD00130814 |
| Chemical Properties | Back Directory | [storage temp. ]
2-8°C | [form ]
lyophilized powder | [color ]
White to off-white | [Water Solubility ]
Soluble in water | [Specific Activity]
≥20units/mg solid |
| Hazard Information | Back Directory | [Uses]
A protease that cleaves proteins on the carboxyl bond of arginine | [Uses]
Clostripain from Clostridium histolyticum has been used as a proteolytic enzyme in perfusate to detect its effect on tube hematocrit. It has also been used in limited proteolysis of DNA polymerase (gp43) of phage T4 (RB69 gp43). | [Biochem/physiol Actions]
Clostripain from Clostridium histolyticum is composed of two polypeptide chains, with molecular masses of 41.7 kDa and 15.4 kDa. Clostripain has a highly restricted substrate specificity for Arg-Xaa peptide bonds. Therefore, clostripain has been explored as a potential enzyme for protein sequencing purposes. It has also been studied as a catalyst for condensation of pharmaceutically important peptides containing Arg-Pro bonds. | [Purification Methods]
Clostripain is isolated from Clostridium histolyticum callogenase by extraction in pH 6.7 buffer, followed by hydroxylapatite chromatography with a 0.1-0.2 M phosphate gradient, then Sephadex G-75 gel filtration with 0.05M phosphate pH 6.7, dialysis and a second hydroxylapatite chromatography (gradient elution with 0.1M 0.3M phosphate, pH 6.7). It has proteinase and esterase activity and is assayed by hydrolysing N-benzoyl-L-arginine methyl ester. [Mitchell & Harrington J Biol Chem 243 4683 1968, Methods Enzymol 19 635 1970.] |
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Sigma-Aldrich
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