STUDIES ON SURFACE DENATURATION OF EGG ALBUMIN

Studies on Surface Denaturation of Egg Albumin*

Bull and Neurath (1) have reported a study of the kinetics of surface denaturation of egg albumin. The protein solutions were shaken in bottles for varying lengths of time, and the amount of denaturation determined. It was not possible, however, in their studies to establish the effect of the extent and rate of formation of surface. The present paper reports a study of surface denaturation occu...

The Temperature Coefficient of the Urea Denaturation of Egg Albumin

Evidence is brought forward to show that at concentrations of urea high enough to split the egg albumin molecule the solubility changes produced by urea are profoundly modified. The degree of precipitation after dialysis is the net result of two changes produced by the urea: the first, normally spoken of as denaturation, which makes the protein insoluble in dilute solution and the second, a spl...

The Denaturation of Egg Albumin by Ultra-violet Radiation

The coagulation of isoelectric egg albumin solutions, on exposure to ultraviolet radiation, involves three distinct processes, (1) the light denaturation of the albumin molecule, (2) a reaction between the light denatured molecule and water which may be similar to heat denaturation but occurs at a lower temperature, and (3), the flocculation of the denatured molecules to form a coagulum. The li...

Denaturation Changes in Egg Albumin with Urea, Radiation, and Heat

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 album...

On the Denaturation of Egg-albumin by Weak Acids in the Presence of Salts.