Isolation and partial characterization of a trypsin inhibitor from wheat endosperm.

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Abstract
Trypsin inhibitors were isolated from wheat endosperm, and a major inhibitor (wheat endosperm trypsin inhibitor-I, WETI-I) was purified by ion-exchange chromatographies on CM-Sephadex and SP-Sephadex, gel filtration on Sephadex G-75 and chromatofocusing on Polybuffer exchanger PBE 94. This inhibitor was a polypeptide composed solely of amino acids and its pI [isoelectric point] value was 9.35. It was homogenous in gel electrophoresis and velocity sedimentation. It showed strong inhibition on bovine trypsin but weak inhibition on bovine .alpha.-chymotrypsin. The MW of the inhibitor was .apprx. 7800 as judged from SDS[sodium dodecyl sulfate]-gel electrophoresis. Evidently, the inhibitor bound trypsin in the molar ratio of 1:1. Certain other properties of the inhibitor, including amino acid composition and UV spectral characteristics are presented.

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