α-糜蛋白酶来源于人类胰腺，α-Chymotrypsin from human pancreas；lyophilized powder, vial of ≥10 BTEE units

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.^[2] Chymotrypsinogen is encoded by the gene CTRB1 and is mapped to 16q23.1 in the human chromosome.^[3]

Application

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.

α-Chymotrypsin from human pancreas has been used to test inhibition by N-alkyl isatins against mammalian serine proteases.^[1]

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.

Unit Definition

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

Analysis Note

由 A1%/280 测定的蛋白质