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