Related Experiment Video
Updated: Aug 8, 2026

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)
Published on: June 20, 2019
Isolation and Characterization of the Multiple 7S Globulins of Soybean Proteins
V H Thanh1, K Okubo, K Shibasaki
1Department of Food Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
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.

