期刊名称：Journal of Nutritional Science and Vitaminology
印刷版ISSN：0301-4800
电子版ISSN：1881-7742
出版年度：1979
卷号：25
期号：1
页码：43-52
DOI：10.3177/jnsv.25.43
出版社：Center for Academic Publications Japan
摘要：Trypsin inhibitors were isolated from wheat germ and two major inhibitors (trypsin inhibitors I and II) were purified by various chromatographies including ion-exchange chromatographies on DEAE-Sephadex and CM-Sephadex as well as gel filtration on Bio-gel and Sephadex. Both inhibitors were polypeptides composed solely of amino acids. In the presence of 1% SDS, inhibitor I showed a single symmetrical sedimentation boundary of 1.6 S and a single band in SDS-gel electrophoresis, but in the absence of SDS, it tended to aggregate. Inhibitor II was found to be homogeneous in gel electrophoresis and velocity sedimentation with or without SDS in the solutions. The molecular weights of inhibitors I and II were approximately 16, 000 and 10, 000, respectively, by SDS-gel electrophoresis. Some other properties of the two inhibitors, including specific inhibitory activities, amino acid compositions and UV spectral properties are presented.
