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Eleven-S globulin heated in the presence of N-ethylmaleimide (NEM) retained its buffer-soluble state. Its gel filtration gave two peaks. Two kinds of electrophoresis indicated that the first peak contained soluble aggregates consisting of intermediary subunits as the major component, and the second peak contained a monomer of acidic subunit and a monomer of intermediary subunit. With an increase in heating time, soluble aggregates polymerized through disulfide bond occurred a little. The temperature of the endothermic peak of 11S globulin heated in the presence of NEM was slightly higher than that in the absence of NEM.

Electrophoretical and differential thermal analysis of soybean 11S globulin heated in the presence of N-ethylmaleimide.