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

Description

Clostripain is a proteolytic enzyme derived from Clostridium histolyticum, which is known for its ability to cleave proteins on the carboxyl bond of arginine. This unique characteristic makes it a valuable tool in various applications across different industries.

Uses

Used in Pharmaceutical Industry:
Clostripain is used as a proteolytic enzyme for limited proteolysis of specific proteins, such as DNA polymerase (gp43) of phage T4 (RB69 gp43). This application aids in the study and understanding of protein structures and functions, which is crucial in drug development and discovery.
Used in Medical Research:
Clostripain is used as a research tool in the detection of its effect on tube hematocrit. This helps in understanding the enzyme's impact on blood components and its potential use in medical diagnostics and therapeutics.
Used in Biochemistry:
As a protease that cleaves proteins on the carboxyl bond of arginine, Clostripain is used in biochemical research to study protein-protein interactions, enzyme mechanisms, and the role of specific amino acid residues in protein function. This knowledge can contribute to the development of new therapeutic agents and a better understanding of biological processes.

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.]