COMPARISON OF THE ACTIVITY AND CONFORMATION CHANGES OF SNase R DURING GUANIDINE DENATURATION
SNase R在胍变性过程中构象与活力变化的比较

The correlation of the activity and conformation changes of SNase R during denaturation by different concentrations of guanidine hydrochloride has been studied by fluorescence and ultraviolet difference sppectrosoopic methods. The denaturation processes of SNase R consist of two first-order reactions in 1.1mol/L. 0.8mol/L. and 0.5mol/L guanidium. but the inactivation process of SNase R were too fast to follow at the same conditions. Moreover, when the denaturation reached equilibrium state, the extent of inactivation of SNase R was much greater than that of either UV difference absorbance or fluorescence intensity changes at the same concentration of guanidium. It seems to suggest that the active site of the enzyme is in a flexible region.