The NMR method previously described by Lambelet et al. (J. Dairy Res. 1989,56,211-222) has been evaluated for the investigation of thermal and acid denaturation of transferrins in aqueous solution.Heating an apoovotransferrin or an apolactoferrin solution resulted in a slight increase in T1-l and an important increase in T2-1 relaxation rates within the denaturation range. The same treatment applied to corresponding iron-saturated proteins resulted in a decrease in these parameters due to modifications of the metal-protein complex accompanying the denaturation. It is proposed that these changes in NMR relaxation parameters can be used to monitor thermal denaturation of transferrins. Acid treatment led to a decrease in relaxation parameters for both apoovotransferrin and iron-saturated (down to pH 4) ovotransferrin. These variations in NMR parameters were related to protein denaturation and indicated that the protein modifications due to acid treatment were different from those occurring during heating.
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