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Analysis Note

Protein determined by A1%/280

Application

α-Chymotrypsin from human pancreas has been used to test inhibition by N-alkyl isatins against mammalian serine proteases.

Human α-chymotrypsin has been used in a study to assess the quantitative structure-activity relationships for organophosphates binding to trypsin and chymotrypsin. Human α-chymotrypsin has also been used in a study to investigate the direct detection of native proteins in biological matrices using extractive electrospray ionization mass spectrometry.

Biochem/physiol Actions

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

General description

α-Chymotrypsin belongs to the trypsin family of serine proteases. It is secreted as an inactive precursor chymotrypsinogen to the intestine. The cleavage of peptide bond at amino acid 148 forms α-chymotrypsin. Chymotrypsinogen is encoded by the gene CTRB1 and is mapped to 16q23.1 in the human chromosome.

Unit Definition

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