- 作者: A. A. Sabourya, A. A. Shamsaeia, A. A. Moosavi-Movahedia and H. Mansuri-Torshizib
- 中文摘要: The interaction of human serum albumin (HAS) with 2,2e-bipyridineglycinato palladium (II) chloride was studied by isothermal titration microcalorimetry at 27 °C and equilibrium dialysis and UV-Vis. Spectrophotometry techniques at temperatures of 27 & 37 °C in 2.5 mM phosphate buffer solution at pH = 7.0. The enthalpy of binding was calculated from binding data, which were obtained from equilibrium dialysis in terms of the Wyman binding potential theory related to the van’t Hoff relation. The enthalpy of HAS unfolding was determined by subtraction of the microcalorimetric enthalpy (binding and unfolding enthalpies) and the enthalpy of binding. The enthalpy of HAS unfolding, due to the binding of that ligand, was 491.43 kJ mol-1.
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