thermodynamic study of human serum albumin upon interaction with ytterbium (iii)
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2013
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Abstract
Complexation reaction between Yb3+ and human serum albumin is examined using isothermal titration calorimetry (ITC). The extension solvation theory was used to reproduce the enthalpies of HAS + Yb3+ interactions over the whole range of Yb3+ concentrations. The binding parameters recovered from this model were attributed to the structural change of HSA. The results show that Yb3+ ions bind to HSA with three equivalent affinity sites. It was found that in the high concentrations of the ytterbium ions, the HSA structure was destabilized.
| Reference Key |
behbehani2013journalthermodynamic
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|---|---|
| Authors | ;G. Rezaei Behbehani;L. Barzegar;M. K. Kiani Savad Koohi;M. Mohebbian;B. Samak Abedi;A. A. Saboury;A. Divsalar |
| Journal | british journal of psychology (london, england : 1953) |
| Year | 2013 |
| DOI |
10.1155/2013/696394
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| URL | |
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