Differential scanning calorimetry (DSC) has been employed to study the thermal denaturation processes of the main protein
fractions of blood serum. These processes have been compared for albumins (nondefatted (HSA) and fatty acid free (HSAf)),
α,β-globulins, γ-globulins, and their mixtures in aqueous (pH 6.5) and buffer (pH 7.2) solutions. The results have indicated
that α,β-globulins inhibit γ-globulins’ aggregation in buffer solutions. The decrease of stability of HSA and HSAf aqueous
solutions has been observed in the presence of γ-globulins. The mixtures of albumins and γ-globulins have revealed the tendency
to ready aggregation in water. Moreover, the results have suggested that neither γ-globulins nor albumins severely change
the stability of α,β-globulins.