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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.
Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.
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.|
|Usage Statement||Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.|