Studies on ovalbumin-s-ovalbumin transformation. I. Some differences noted between the properties of ovalbumin and s-ovalbumin in native state.

To study the mechanism of the formation of the heat-stable form of ovalbumin (s-ovalbumin), comparisons were made about the properties of ovalbumin and s-ovalbumin in native state. Although gross structural difference could not be found, some minor differences were clearly noted in some cases such as the DEAE-cellulose chromatographic elution pattern, the isoelectric focusing and the titration curve of both proteins. All these results seem to show that changes in the surface charge occur during ovalbumin-s-ovalbumin transformation.