Trypsin Inhibitor, Soybean

Soybean trypsin inhibitor (SBTI) first crystallized by Kunitz (1945) is one of several such inhibitors found in soybeans. A single Arginine-Isoleucine bond is cleaved by trypsin, a covalent bimolecular complex of inhibitor and trypsin results. On dissociation either virginal or modified inhibitor appears. Activity: 1mg inhibits > 1.2 mg of trypsin, (1mg trypsin > 180 TAME units, 10,350 BAEE units, 3450 USP/NF units), Unit Definition: One Unit hydrolyzes one umole of TAME/min. at 25ºC, pH 8.2, in the presence of 0.1M calcium. A280@mg/ml: As reported, Storage and Stability: Lyophilized product is stable for 6 months after receipt at 4°C. For maximum recovery of product, centrifuge the original vial prior to removing the cap.