ABSTRACTThermal association‐dissociation behavior of soybean 11S globulin was investigated by sucrose density gradient centrifugation and polyacrylamide gel electrophoresis. Soluble aggregates with a molecular weight of 8 × 106were formed when 0.5% and 5% protein solutions were heated for 1 min at 100°C. At the lower protein concentration, subsequent heating caused disappearance of the soluble aggregate followed by complete dissociation into acidic and basic subunits. At the higher concentration, however, subsequent heating caused formation of highly polymerized aggregates, and gel was formed after 5 min of heating. The soluble aggregates appear to be transient intermediates in the course of gel formation of 11S globu