Abstract
Native subunit proteins of glycinin, the acidic and the basic subunits designated as ASS1+2, AS2+3, AS4, AS5, and AS6, and BS, respectively, were isolated by DEAE-Sephadex A-50 column chromatography in the presence of 6M urea and 0.2M 2-mercaptoethanol.
Reconstitution of intermediary subunits involving a disulfide bridge from native acidic and basic subunits was investigated. Formation of the intermediary subunit was observed in combinations between BS and each acidic subunit except AS6. The yields of the reconstituted intermediary subunits differed from one another.
Further, formation of the intermediary complexes was observed when native acidic and basic subunits of soybean glycinin and sesame 13S globulin, respectively (or reverse combi-nations), were mixed under reductively denatured condition and subjected to the reconstitution procedure. Considerring the overall evidence, we may conclude that the complexes are probably a hybrid intermediary subunit.
