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A Thermodynamic Study on the Binding of Human Serum Albumin with Lanthanum Ion
Author(s) -
Rezaei Behbehani G.,
Divsalar A.,
Saboury A. A.,
Faridbod F.,
Ganjali M. R.
Publication year - 2010
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201090047
Subject(s) - chemistry , isothermal titration calorimetry , solvation , human serum albumin , lanthanum , cooperativity , calorimetry , enthalpy , titration , thermodynamics , serum albumin , ion , inorganic chemistry , chromatography , organic chemistry , biochemistry , physics
Thermodynamics of the interaction between lanthanum(III) ion, La 3+ , and human serum albumin (HSA), was investigated at pH 7.0 and 300 K in Tris‐HCl buffer by isothermal titration calorimetry. A solvation model was used to reproduce the enthalpies of HSA interaction with La 3+ . The solvation parameters recovered from our new model were attributed to the structural change of HSA and its biological activity. The interaction of HSA with La 3+ showed a set of two binding sites with negative cooperativity.