z-logo
Premium
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom