作者: Kazuo Shibasaki , Vu Huu Thanh , Kazuyoshi Okubo
DOI:
关键词: Tris 、 Column chromatography 、 Chemistry 、 Glycine 、 Chromatography 、 Fraction (chemistry) 、 Globulin 、 Sephadex 、 Ionic strength 、 Hydroxymethyl
摘要: Two major proteins (the 7S and 11S globulins) of soybean (Glycine max) were simultaneously isolated by a simple method based on their different solubilities in dilute tris (hydroxymethyl)aminomethane buffers. The purified globulins, which represented essentially the entire protein fraction capable dimerization at 0.1 ionic strength, fractionated into five components diethylaminoethyl Sephadex A-50 column chromatography. characterized disc-electrophoresis.