Abstract
The renaturation in the quarternary structure of major protein component was observed by gel electrophoresis, when the soybean protein was neutralyzed to pH 8.6, after heating at alkaline or acidic pH, under which the conformational change occured.
The difference spectra and ORD measurement in isolated 11S protein solution showed that the protein was renatured almost completely by neutralyzing the protein solution treated at the pH below 11.22 and partially renatured by neutralyzing the protein solution treated at the pH over 11.22 or at pH 2.35.
