The acidic and the basic subunits were shown to be present in equimolar amounts in the 11 S globulin molecule by the densitometric scanning of the SDS gel and the molecular weight consideration. The four acidic subunits (A₁, A₂, A₃ and A₄) were found to be present in the approximate molar ratio of 1:1:2:2. Four basic subunits separated and designated as B₁, B₂, B₃ and B₄ based on the relative mobilities in the acidic gel in 7M urea were found to be present in the approximate molar ratio of 1:1:2:2. The four basic subunits were fractionated in approximately same amounts into three different peaks, peak I (B₁ and B₂), peak II (B₃) and peak III (B₄) by CM-Sephadex C-50 column chromatography in the presence of 6M urea. Three kinds of intermediary subunits of 11 S globulin were fractionated with DEAE-Sephadex A-50 in the absence of reducing agents in 6M urea, and disulfide bonds appeared to participate in the binding between the acidic and the basic subunits in the molar ratio of 1:1 with the following combinations; A₁ and A₂ combined with B₃, A₃ with B1 and B₂, and A₄ with B₄. In view of the above results and molecular weight consideration, a new model of subunit structure was proposed for 11 S globulin.

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