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The denaturation of ovalbumin by heat at pH 2-3 hus been studied by following the changes in optical rotation, viscosity, solubility at the isoelectric point, and amount of aggregated protein observed in the ultracentrifuge. The laevorotation and reduced viscosity of heated solutions of ovalbumin increase with ionic strength and protein concentration. This effect is related to the state of aggregation of the denatured protein and not to the extent of denaturation as measured by changes in solubility. The initial denaturation step is irreversible but does not involve the extensive unfolding observed in urea solutions.

Studies on Ovalbumin I. Denaturation By Heat, and the Heterogeneity of Ovalbumin