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A New Approach for Thermodynamic Study on the Binding of Human Serum Albumin with Cerium Chloride
Rezaei Behbehani, G.,Divsalar, A.,Saboury, A.A.,Faridbod, F.,Ganjali, M.R. Korean Chemical Society 2009 Bulletin of the Korean Chemical Society Vol.30 No.6
Thermodynamics of the interaction between Cerium (III) chloride, $Ce^{3+}$, with Human Serum Albumin, HSA, was investigated at pH 7.0 and $27\;{^{\circ}C}$ in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by $Ce^{3+}$. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA with $Ce^{3+}$ showed a set of two binding sites with negative cooperativity. $Ce^{3+}$ interacts with multiple sites on HSA affecting its biochemical and biophysical properties.
A New Approach for Thermodynamic Study on the Binding of Human Serum Albumin with Cerium Chloride
G. Rezaei Behbehani,A. Divsalar,A. A. Saboury,F. Faridbod,M. R. Ganjali 대한화학회 2009 Bulletin of the Korean Chemical Society Vol.30 No.6
Thermodynamics of the interaction between Cerium (III) chloride, Ce3+, with Human Serum Albumin, HSA, was investigated at pH 7.0 and 27 oC in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by Ce3+. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA withCe3+ showed a set of two binding sites with negative cooperativity. Ce3+ interacts with multiple sites on HSA naffecting its biochemical and biophysical properties