Behavior of the 11S Protein of Soybeans in Acid Solutions. I. Effects of pH, Ionic Strength and Time on Ultracentrifugal and Optical Rotatory Properties²

Isolation, Purification, and Characterization of the Oligomeric Seed Globulin fromAmaranthus hypochondriacus

“…The finding was consistent with the 15 ) and Koshiyama 28) postulated that the dissociation phenomenon was the result of electrostatic repulsion between subunits of non-covalently linked protein moieties. This finding is significant in view of the fact that attractive forces responsible for holding protomers together involve such weak secondary forces as hydrogen bonding, and hydro- phobic and/or van der Waals interactions.…”

Isolation of Soybean 11S Globulin by Isoelectric Precipitation and Sephacryl S-300 Gel Filtration Chromatography: A New Purification Technique

“…As could be noted in Fig. 2 (Lane B), the globulin underwent an alkaline-pH-induced dissociation that is characteristic of the 11 S soybean globulin as previously described by Wolf et al 14 ) and Kitamura et al…”

The action of pepsin on the reserve proteins of some leguminous seeds

“…The aforementioned proteins are dissociated into subunits in acid milieu [6,71 and an essential change in the optical rotation of soybean 11-S protein occurs at pH 2. Both vetch reserve proteins and soybean 1 I-S protein are hydrolyzed completely and with the same rate which is considerably higher than under the action of trypsin and chymotrypsin.…”