Hen egg ovalbumin is a mixture of three kinds ofproteins, Au A2, and A3 with two, one, and no phosphoryl residues, respectively.These three proteins were obtained by acid phosphatase treatment and then chromatography on a DEAEcellulofme AHcolumn.The isoelectric points of Al9 A2, and A3 were found by isoelectric focusing to be pH 4.75, 4.89, and 4.94, respectively.The denaturation temperature of each protein was examined by differential scanning calorimetry at its own isoelectric point and at pH 4.65.At both pHs, A3 had a lower denaturation temperature than A2or A1#The surface tension of an A3solution reached a constant more quickly than At or A2after formation of a new surface of the solution.These results indicate that the completely dephosphorylated ovalbumin A3 is more susceptible to heat and surface denaturation than phosphorylated ovalbumin is.The difference in the heat aggregation patterns of A1? A2, and A3solutions at different pH or salt concentrations showed that the electrostatic-repulsive force is
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Kitabatake et al. (1988) studied this question.