Abstract
Thermal denaturation of cytochromes c of horse, cow, and Candida krusei in aqueous guanidine hydrochloride in the neutral pH region was studied by means of absorption and optical rotation measurements. The values of standard free energy change upon denaturation were estimated over the temperature range from 3 to 51°C. Large differences in the heat capacity of the native and denatured states amounting to several kcal/mol. deg were obtained for all three kinds of cytochromes c. These lead to a change in the sign of both the enthalpy and entropy change of denaturation, with maximum stability of the native state at l2°C for horse and bovine cytochromes c and at 9°C for Candida krusei.
