Thermodynamic Study of the Binding of Mercury Ion to Human Growth Hormone at Different Temperatures

被引：0
作者：
E. Tazikeh Lemeski
G. Rezaei Behbehani
A. A. Saboury
M. Monajjemi
R. Zafar Mehrabian
M. Ahmadi Golsefidi
H. Rajabzadeh
M. T. Baei
S. Hasanzadeh
机构：
[1] Islamic Azad University,Department of Chemistry, Science and Research Branch
[2] Takestan Branch,Department of Chemistry
[3] Islamic Azad University,Institute of Biochemistry and Biophysics
[4] University of Tehran,Department of Chemistry
[5] Gorgan Branch,Department of Chemistry
[6] Islamic Azad University,Minoodasht Branch
[7] Dezful Branch,Young Researchers Club
[8] Islamic Azad University,undefined
[9] Islamic Azad University,undefined
[10] Gorgan Branch,undefined
[11] Islamic Azad University,undefined
来源：
Journal of Solution Chemistry | 2011年 / 40卷
关键词：
Human growth hormone (hGH); Isothermal titration calorimetry (ITC); Solvation model; Mercury ion; Metal binding;
D O I：
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中图分类号：
学科分类号：
摘要：
The interaction of human growth hormone (hGH) with the divalent mercury ion was studied by isothermal titration calorimetry at two temperatures of 27 °C and 37 °C in aqueous solutions. We found that there is a set of two identical and non-interacting binding sites for Hg2+ ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 4.2 mmol⋅L−1 and −14.8 kJ⋅mol−1 at 27 °C and 5.1 mmol⋅L−1 and −14.2 kJ⋅mol−1 at 37 °C, respectively. The results obtained indicate that the stability of the protein increases due to the binding of mercury ions using the extended solvation theory.
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页码：575 / 586
页数：11
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