[An alcohol-soluble trypsin inhibitor from beans]

Abstract

An ethanol soluble protein-trypsin inhibitor was isolated from kidney bean seeds. The inhibitor purification included gel chromatography of ethanol soluble proteins on Sephadex G-75 and affine chromatography on immobilized trypsin and chymotrypsin. The inhibitor suppressed activites of trypsin, chymotrypsin and in part trypsin-chymotrypsin activity of pronase but did not influence subtilizin. The inhibitor at a dose of 15-17.5 mug decreased by 50% the activity of 100 mug trypsin. By isoelectric focusing it was shown that the inhibitor isolated from kidney beans consisted of four isoinhibitors with pH of 4.3, 4.5, 4.7, and 4.9.