Some Differences Noted between the Properties of Ovalbumin and s-Ovalbumin in Native State

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Abstract
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.

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