Cereal Chem 45:405 - 412.  |  VIEW ARTICLE
Chromatographic and Sedimentation Behavior of a Purified 7S Protein in Soybean Globulins.

I. Koshiyama. Copyright 1968 by the American Association of Cereal Chemists, Inc. 

A 7S protein of soybean globulins isolated by cooling an aqueous meal extract, adding CaCl2 and performing gel filtration with Sephadix G-100 and G-200, was homogeneous ultracentrifugally, electrophoretically, and chromatographically on hydroxylapatite and Sephadex G-200. This preparation corresponded to fraction D of the chromatogram of soybean globulins on hydroxylapatite by Wolf and Sly (Arch. Biochem. Biophys. 110; 47; 1965) and peak 3 in gel filtration of water-extractable soybean proteins by Hasegawa et al. (Agr. Biol. Chem. 27: 878; 1968). This protein underwent quantitatively a reversible 7S- 9S isomerization with change of ionic strength from micron = 0.1 to micron = 0.5. In 0.01N HCl, this protein separated into two small components, but in a small amount of NaCl they associated into only one peak having a sedimentation coefficient of approximately 7S quantitatively. The isoelectric point was at pH 4.90.