Isolation and Partial Characterization of a Trypsin Inhibitor form Wheat Endosperm

概要

論文の詳細を見る
Tyypsin 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 pl value was 9.35. It was found to be homogeneous in gel electrophoresis and velocity sedimentation. It showed strong inhibition on bovine trypsin but weak inhibition on bovine a-chymotrypsin. The molecular weight of the inhibitor was approximately 7, 800 as judged from SDS-gel electrophoresis. This finding, along with the trypsin inhibition data, suggested that 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.
財団法人学会誌刊行センターの論文