Thermal investigation of Human Serum Albumin upon Interaction with Ytterbium (III)
نویسندگان
چکیده
Article history: Received January 01, 2012 Received in Revised form January 10, 2012 Accepted 13 January 2012 Available online 19 January 2012 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. © 2012 Growing Science Ltd. All rights reserved.
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