Thermodynamic Study of the Binding of Mercury Ion to Human Growth Hormone at Different Temperatures
Yazarlar (9)
E. Tazikeh Lemeski Islamic Azad University, Science And Research Branch, İran
G. Rezaei Behbehani Islamic Azad University, Takestan Branch, İran
A. A. Saboury
University of Tehran, İran
Prof. Dr. Majıd MONAJJEMI Islamic Azad University, Science And Research Branch, İran
R. Zafar Mehrabian Islamic Azad University, Gorgan Branch, İran
M. Ahmadi Golsefidi Islamic Azad University, Gorgan Branch, İran
H. Rajabzadeh Islamic Azad University, Dezful Branch, İran
M. T. Baei Islamic Azad University, İran
S. Hasanzadeh Islamic Azad University, Gorgan Branch, İran
Makale Türü Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı Journal of Solution Chemistry (Q3)
Dergi ISSN 0095-9782 Dergi Bilgileri (2011)
Makale Dili İngilizce Basım Tarihi 04-2011
Cilt / Sayı / Sayfa 40 / 4 / 575–586 DOI 10.1007/s10953-011-9668-4
Makale Linki http://www.scopus.com/inward/record.url?eid=2-s2.0-79958048253&partnerID=MN8TOARS
UAK Araştırma Alanları
Özet
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. © 2011 Springer Science+Business Media, LLC.
Anahtar Kelimeler
Human growth hormone (hGH) | Isothermal titration calorimetry (ITC) | Mercury ion | Metal binding | Solvation model
BM Sürdürülebilir Kalkınma Amaçları
Atıf Sayıları
Web of Science 7
Scopus 9
Thermodynamic Study of the Binding of Mercury Ion to Human Growth Hormone at Different Temperatures

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