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  • 1 A. Chełkowski Institute of Physics, Department of Medical Physics, University of Silesia, ul. Uniwerytecka 4, 40-007 Katowice, Poland
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Abstract  

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.

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