Author(s): Mohammad Mirzaie | Lyla Barzegar | Gholamreza Rezaei Behbehani | Ali Akbar Saboury
Journal: Current Chemistry Letters
ISSN 1927-7296
Volume: 1;
Issue: 1;
Start page: 35;
Date: 2012;
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Keywords: Isothermal Titration Calorimetry | Human Serum | Yb3+ Ion | Binding Parameters
ABSTRACT
In this paper complexation reaction between Yb3+ and Human serum albumin is examined using isothermal titration calorimetry (ITC). The extended solvation model 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.
Journal: Current Chemistry Letters
ISSN 1927-7296
Volume: 1;
Issue: 1;
Start page: 35;
Date: 2012;
VIEW PDF
DOWNLOAD PDF Original pageKeywords: Isothermal Titration Calorimetry | Human Serum | Yb3+ Ion | Binding Parameters
ABSTRACT
In this paper complexation reaction between Yb3+ and Human serum albumin is examined using isothermal titration calorimetry (ITC). The extended solvation model 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.
