| Literature DB >> 16659250 |
V H Thanh1, K Okubo, K Shibasaki.
Abstract
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 7S globulins, which represented essentially the entire 7S soybean protein fraction capable of dimerization at 0.1 ionic strength, were fractionated into five components by diethylaminoethyl Sephadex A-50 column chromatography. The five 7S components were characterized by disc-electrophoresis.Entities:
Year: 1975 PMID: 16659250 PMCID: PMC541290 DOI: 10.1104/pp.56.1.19
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340