Not available outside of the UK & Ireland.

Application

α-Chymotrypsin from bovine pancreas is used for the following applications:Protein Identification by mass spectrometry (MS)The isolation and characterization of myosin heavy chainsToxin preparationThe incubation of infected and uninfected cells for analysis of cellular proteins by SDS-PAGEα-Chymotrypsin from bovine pancreas (BPC) may be used as a catalyst in the preparation of tetrahydroquinoline derivatives by Povarov reaction.

Biochem/physiol Actions

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

α-Chymotrypsin from bovine pancreas is stabilized by Ca²⁺ and catalyzes the hydrolysis of peptide bonds in particular the amino acids tyrosine, phenylalanine, tryptophan, and leucine at their C-terminal side. α-Chymotrypsin is inhibited by Cu²⁺ and Hg.

General description

Chymotrypsin (Chy) is a serine protease. It corresponds to a molecular weight of 25.7 kDa and is widely used in pharmaceutical industry. It is synthesized in pancreas from chymotrypsinogen and require calcium for this conversion.

α-Chymotrypsin from bovine pancreas (bovine pancreatic α-chymotrypsin, CHT) is an enzyme protein. The influence of varying concentrations of organic solvents like ethanol, 1,4-dioxane and acetonitrile on CHT has been reported.

Other Notes

View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer

Unit Definition

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