9028-00-6

Basic information

• Product Name: CLOSTRIPAIN
• Synonyms: ENDOPROTEINASE-ARG-C;EC 3.4.22.8;CLOSTRIPAIN;CLOSTRIDIOPEPTIDASE B;IUB: 3.4.22.8;PROTEINASE;clostripain from clost. histolyticum;CLOSTRIPAIN FROM CLOST. HISTOLYTICUM >1
• CAS NO: 9028-00-6
• Molecular Weight: 0
• EINECS: 232-822-2
• Mol File: 9028-00-6.mol
• Article Data: 0

Chemical Properties

• Appearance: /lyophilized powder
• Storage Temp.: 2-8°C
• Water Solubility: Soluble in water
• CAS DataBase Reference: CLOSTRIPAIN(CAS DataBase Reference)
• NIST Chemistry Reference: CLOSTRIPAIN(9028-00-6)
• EPA Substance Registry System: CLOSTRIPAIN(9028-00-6)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• F: 3-10-21
• Hazardous Substances Data: 9028-00-6(Hazardous Substances Data)

Usage

Uses

Different sources of media describe the Uses of 9028-00-6 differently. You can refer to the following data:
1. A protease that cleaves proteins on the carboxyl bond of arginine
2. 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.]