α-chymotrypsin 40-50 unit/mg, 1 g
Chymotrypsin preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine, and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. In addition to bonds involving aromatic amino acids, chymotrypsin catalyzes at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues. a-Chymotrypsin is a protein consisting of 241 amino acid residues. The molecule has three peptide chains: an A chain of 13 residues, a B chain of 131 residues, and a C chain of 97 residues.
α-Chymotrypsin is used for treating pancreatic insufficiency and in traumatology.
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Enzymes | Inhibitors | Substrates
|Application Notes||α-Chymotrypsin is used for treating pancreatic insufficiency and in traumatology.|
|Base Catalog Number||10046191|
|Biochemical Physiological 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.|
|Pack Size||1 g|
|Personal Protective Equipment||Dust mask, Eyeshields, Faceshields, Gloves|
|Preparation Method||Produced from 3x crystallized chymotrypsinogen|
|Safety Symbol||GHS07, GHS08|
|Specific Activity||≥40 u/mg protein|
|Unit Definition||One unit will hydrolyze 1 umole of N-benzoyl-L-tyrosine ethyl ester per minute at pH 7.8 and 25 °C.|