| Makale Türü | Özgün Makale (ESCI dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Journal of Solution Chemistry | ||
| Dergi ISSN | 0095-9782 Wos Dergi Scopus Dergi | ||
| 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 | ||
| 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 |
| Atıf Sayıları | |
| Web of Science | 6 |
| Scopus | 8 |
| Dergi Adı | JOURNAL OF SOLUTION CHEMISTRY |
| Yayıncı | Springer |
| Açık Erişim | Hayır |
| ISSN | 0095-9782 |
| E-ISSN | 1572-8927 |
| CiteScore | 2,3 |
| SJR | 0,279 |
| SNIP | 0,671 |