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C1012 Sigma

α-Chymotrypsin, Inactivated from bovine pancreas

Type VI (Inactivated with DFP), lyophilized powder, <0.2 units/mg protein

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Properties

Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Chymotrypsin, alpha-,
type   Type VI (Inactivated with DFP)
form   lyophilized powder
mol wt   mol wt 25 kDa
purified by   3× crystallization
storage temp.   −20°C
Gene Information   cow ... CTRB1(618826)

Description

Analysis Note

Protein determined by A1%/280

Biochem/physiol Actions

α-Chymotrypsin is a serine peptidase. It has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, 10 mM Cu2+ and Hg2+.

Unit Definition

One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

Price and Availability

Suggested Laboratory Gloves


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Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
1
RTECS 
GC3050000

Documents

Certificate of Analysis

Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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