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ABSTRACT
The adsorption and conformation transformation of bovine serum albumin (BSA) on a reversed-phase octadecylsilyl group based on silica reversed-phase chromatographic column were studied in the temperature of 12–50°C. The thermodynamic and extrathermodynamic data were determined and compared to each other. The results showed that when temperature was below 20°C, BSA existed only in its native conformation state A; whereas when temperature was over 20°C, parts of the conformation state A changed to state B. In transformation process, endothermal and nonspontaneous reaction occurred and the entropy change was favorable for the transformation; while in adsorption process, the reaction was exothermal and spontaneous and driven simultaneously by enthalpy and entropy change. The compensation temperature in the conformation transformation of BSA was significantly less than that in the adsorption of the two conformation states. This phenomenon demonstrated the big difference during the two processes.
GRAPHICAL ABSTRACT
