Thermodynamic Study of Human Serum Albumin upon Interaction with Ytterbium (III) | Zendy

G. Rezaei Behbehani | Zendy; L. Barzegar | Zendy; Maryam Koohi | Zendy; M. Mohebbian | Zendy; B. Samak Abedi | Zendy; Ali Akbar Saboury | Zendy; Adeleh Divsalar | Zendy

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Thermodynamic Study of Human Serum Albumin upon Interaction with Ytterbium (III)

Author(s) -

G. Rezaei Behbehani,

L. Barzegar,

Maryam Koohi,

M. Mohebbian,

B. Samak Abedi,

Ali Akbar Saboury,

Adeleh Divsalar

Publication year - 2012

Publication title -

journal of chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.436

H-Index - 50

eISSN - 2090-9063

pISSN - 2090-9071

DOI - 10.1155/2013/696394

Subject(s) - chemistry , isothermal titration calorimetry , ytterbium , human serum albumin , solvation , titration , serum albumin , ion , inorganic chemistry , chromatography , organic chemistry , biochemistry , physics , optoelectronics , doping

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

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