Thermodynamic Study of Human Serum Albumin upon Interaction with Ytterbium (III)
Keyword(s):
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.
2016 ◽
Vol 52
(3)
◽
pp. 443-446
Keyword(s):
2013 ◽
Vol 155
(1)
◽
pp. 150-158
◽
2015 ◽
Vol 232
◽
pp. 77-84
◽
2005 ◽
Vol 310
(1-3)
◽
pp. 51-58
◽
2017 ◽
Vol 36
(7)
◽
pp. 1747-1763
◽
2013 ◽
Vol 42
(5)
◽
pp. 1005-1017
◽