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C9134 Sigma-Aldrich

α-Chymotrypsin−Agarose from bovine pancreas

lyophilized powder, 2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)

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Description

Application

α-Chymotrypsin agarose from bovine pancreas has been used to study the purification and characterization of glucoamylase. α-Chymotrypsin agarose from bovine pancreas has also been used in a study to investigate molecular modeling for the design of a biomimetic chimeric ligand.

Packaging

50, 100 units in poly bottle

Biochem/physiol Actions

α-Chymotrypsin is a serine peptidase and 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. The 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+.

Serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the bond.

Unit Definition

One unit will hydrolyze 1.0 μmole of N-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 8.0 at 30 °C.

Physical form

Stabilized with lactose

Analysis Note

Protein determined by A1%/280

Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis

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Protocols & Articles

Related Content

Enzymes & Proteins

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

Peer-Reviewed Papers
15

References

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