title: DENATURATION CHANGES IN EGG ALBUMIN WITH UREA, RADIATION, AND HEAT.
abstract: The extent of urea denaturation depends on the concentration of protein and urea and also on the temperature of the solution. Egg albumin solutions (0.9 per cent) are not denatured by 20 per cent urea, denature slowly with 25 per cent urea, and denature rapidly with 35 per cent urea at room temperature. At a higher temperature 30 per cent urea is rapidly effective. Denaturation of the egg albumin molecule by radiation or by heat is accompanied by structural changes as evidenced by optical rotation values, but is not accompanied by association or dissociation of the molecule in the pH range outside the zone in which aggregation follows denaturation. Denaturation of the egg albumin molecule by urea produces no change in optical rotation until the concentration of urea is high enough to dissociate the molecule. In the presence of urea a urea-protein complex is formed in which the protein is denatured but cannot flocculate because of the dispersive action of the urea. This prevents flocculation of proteins exposed to radiation and subsequent heating to 40 degrees C. as the urea-protein complex is not broken down at a temperature of 40 degrees C. The presence of urea therefore prevents the flocculation of proteins denatured by radiation. The urea-protein complex is broken down by heating to 55-58 degrees C. so that the molecules aggregate at a temperature below the temperature of rapid heat denaturation. This appears to be an acceleration of heat denaturation or a lowering of the heat denaturation temperature, but in reality is an effect of heat on the urea-protein complex which frees the urea-denatured protein and permits its aggregation.
authors.affiliation: Division of Biological Sciences, The University of Rochester, Rochester, New York.
authors.forename: J H
authors.initials: JH
authors.lastname: Clark