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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 30, Number 6
BKCSDE 30(6)
June 20, 2009 

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
Human Serum Albumin, Isothermal titration calorimetry, Cerium (III) chloride.
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 with Ce3+ showed a set of two binding sites with negative cooperativity. Ce3+ interacts with multiple sites on HSA affecting its biochemical and biophysical properties.
1262 - 1266
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