Abstract
DURING work on the heat denaturation of ovalbumin at pH 3, it was found, from measurements of the changes in solubility and in the amount of aggregated protein observed in the ultracentrifuge, that the ovalbumin behaved as a mixture of two proteins with different rates of denaturation. This was confirmed by heating an ovalbumin solution until about 80 per cent of the protein had become insoluble at the isoelectric point, removing the denatured protein and measuring the rate of solubility loss of the remaining protein at pH 3. This was found to be less than a quarter of the rate of denaturation of whole ovalbumin.
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References
Creeth, J. M., Nichol, L. W., and Winzor, D. J., J. Phys. Chem., 62, 1546 (1958).
Huggins, C., Tapley, D. F., and Jensen, E. V., Nature, 167, 592 (1951).
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SMITH, M., BACK, J. Modification of Ovalbumin in Stored Eggs detected by Heat Denaturation. Nature 193, 878–879 (1962). https://doi.org/10.1038/193878a0
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DOI: https://doi.org/10.1038/193878a0
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