Trypsin-chymotrypsin inhibitor

Trypsin-chymotrypsin inhibitor belongs to the family of plant protease inhibitors. It is mainly found in the legume (Fabaceae) and cereal (Poaceae) families. Trypsin-chymotrypsin inhibitor consists of many internal disulfide bonds between conserved Cys residues, which maintains structural stability and active conformation of the inhibitory loops. Trypsin-chymotrypsin has anticarcinogenic properties.

Highly cross-linked with seven disulfide bridges, Bowman-Birk inhibitor has spatially distinct domains for trypsin and chymotrypsin inhibition.

Trypsin-chymotrypsin inhibitor from Glycine max (soybean) has been used for flow cytometric separase activity assay. It has also been used to inhibit trypsin and chymotrypsin for in vitro gastrointestinal (GI) digestion studies.

Bowman Birk protease inhibitor prevents radiation-induced carcinogenesis by a reduction of incorrect DNA repairs, resulting in a reduced amount of dicentric chromosomes.

Lyophilized powder containing phosphate buffer salts, pH 7.6

1 mg protein will inhibit ≥0.5 mg trypsin with activity of ~10,000 BAEE units per mg protein or ≥1.0 mg chymotrypsin with activity of ~40 BTEE units per mg protein.

One trypsin unit = ΔA₂₅₃ of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C. Reaction volume = 3.2 mL (1 cm light path).

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