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A high performance method for thermodynamic study on the binding of human serum albumin with erbium chloride
Authors:G. Rezaei Behbehani  A. Divsalar  A. A. Saboury  F. Faridbod  M. R. Ganjali
Affiliation:(1) Chemistry Department, Imam Khomeini International University, Qazvin, Iran;(2) Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;(3) Department of Biological Sciences, Tarbiat Moallem University, Tehran, Iran;(4) Departments of Chemistry, University of Tehran, Tehran, Iran
Abstract:Thermodynamics of the interaction between erbium(III) chloride, Er3+, with human serum albumin (HSA), was investigated at pH 7.0 and in phosphate buffer by isothermal titration calorimetry. Our recently, solvation model was used to reproduce the enthalpies of HSA interaction by Er3+ over a broad range of metal ion concentration. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The binding parameters for the interaction of Er3+ and HSA indicate that the concentrations of Er3+ have no significant effects on the structure of HSA.
Keywords:erbium(III) chloride  human serum albumin  isothermal titration calorimetry
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