Abstract
Summary The denaturation of egg albumin, in the pH range of 0.9–3.4, over the temperature range 25.0–44.4°C., has been found to follow first-order kinetics, over a wide range of initial protein concentrations and for a wide range of the total denaturation process. Two distinct ways of denaturation have been detected. The first involves the suppression of the dissociation of one hydrogen ion in the protein molecule, while the secon involves two such suppressions. In a moderately acid solution, only the first such dissociation is of significance, while the second dissociation enters into prominence in more acid regions. From the respective rate constants, the apparent heats of activation, ΔH*, were found to be 36.7 and 50.0 kcal./mole.
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