The multiple 7S globulins composed of two fractions (A and B) in the electrophoresis with Davis` method were isolated at different stages of the soybean seed development. Electrophoresis of their subunits liberated in PAWU solvent [phenol-acetic acid-water (2 : 1 : 1) solution plus 5M urea] yielded 4 major bands. Observation of both the electrophoretic bands of the multiple 7S fractions(7S-A and 7S-B) and those of their subunits was suggestive of a similarity of the subunit pattern between two 7S fractions. The two fractions in multiple 7S globulins were isolated witb DEAE-Sephadex A-50 column(2.0×100㎝) chromatography. They were separated into 2 fractions in a linear gradient concentration of 0.28 to 0.40M NaCl with phosphate buffer (pH 7.8) containing 10mM β-mercaptoethanol(ME). The isolated protein was dissociated into subunits with two different solvent systems; m PAWU solvent and in Tris-HCl buffer(pH 8.0) containing 1% sodium dodecyl sulfate (SDS) and 40mM ME. The dissociated subunits were subjected to electrophoresis in PAWU-treated 7.5% acrylamide gel and in 1% SDS-treated 5.6% acrylamide gel. In PAWU gel electrophoresis, total 7S globulin was separated into 5 major bands, two of which were occupied in common by two 75 fractions(7S-A and 7S-B). In SDS gel electrophoresis, total 7S globulin was separated into 7 major bands, three of which were overlapped with the subunit of the two 7S fractions. The above results alluded us to the presence of a common and/or similar subunit between the multiple 7S globulins.