A Microcalorimetry Study of the Binding of Nickel Ion by Human Growth Hormone

A binding study of nickel ions by a new recombinant human Growth Hormone (hGH), produced as an injected drug, has been done at 27˚C in NaCl solution (50 mM) using an isothermal titration calorimetry. There is a set of three identical and non-interacting binding sites for nickel ions. The intrinsic d...

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Main Authors: Ali Akbar Saboury, Safoura Amiri
Format: Article
Language:English
Published: Iranian Institute of Research and Development in Chemical Industries (IRDCI)-ACECR 2010-12-01
Series:Iranian Journal of Chemistry & Chemical Engineering
Subjects:
Online Access:http://www.ijcce.ac.ir/article_6397_916950c3c45b35ab9e7739e6a7bb308b.pdf
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author Ali Akbar Saboury
Safoura Amiri
author_facet Ali Akbar Saboury
Safoura Amiri
author_sort Ali Akbar Saboury
collection DOAJ
description A binding study of nickel ions by a new recombinant human Growth Hormone (hGH), produced as an injected drug, has been done at 27˚C in NaCl solution (50 mM) using an isothermal titration calorimetry. There is a set of three identical and non-interacting binding sites for nickel ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 40 μM and -16.5 kJ/mol, respectively. Thermodynamic parameters of nickel ion binding are compared to the other metal ions. The molar entropy of binding is 29.3 J K-1 mol-1 for Ni2+, less than Cu2+ and more than other metal ions, means that the disorder of the protein structure due to the binding of nickel ions is more than to the other ion metals, except Cu2+. It is expected that nickel ions can prevent from the aggregation of the protein.
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spelling doaj.art-2f71f64f747e4d96beb68f5b403e528d2022-12-22T03:16:46ZengIranian Institute of Research and Development in Chemical Industries (IRDCI)-ACECRIranian Journal of Chemistry & Chemical Engineering1021-99861021-99862010-12-0129431366397A Microcalorimetry Study of the Binding of Nickel Ion by Human Growth HormoneAli Akbar Saboury0Safoura Amiri1Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, I.R. IRANInstitute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, I.R. IRANA binding study of nickel ions by a new recombinant human Growth Hormone (hGH), produced as an injected drug, has been done at 27˚C in NaCl solution (50 mM) using an isothermal titration calorimetry. There is a set of three identical and non-interacting binding sites for nickel ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 40 μM and -16.5 kJ/mol, respectively. Thermodynamic parameters of nickel ion binding are compared to the other metal ions. The molar entropy of binding is 29.3 J K-1 mol-1 for Ni2+, less than Cu2+ and more than other metal ions, means that the disorder of the protein structure due to the binding of nickel ions is more than to the other ion metals, except Cu2+. It is expected that nickel ions can prevent from the aggregation of the protein.http://www.ijcce.ac.ir/article_6397_916950c3c45b35ab9e7739e6a7bb308b.pdfhuman growth hormonenickel ionmetal bindingtitration calorimetry
spellingShingle Ali Akbar Saboury
Safoura Amiri
A Microcalorimetry Study of the Binding of Nickel Ion by Human Growth Hormone
Iranian Journal of Chemistry & Chemical Engineering
human growth hormone
nickel ion
metal binding
titration calorimetry
title A Microcalorimetry Study of the Binding of Nickel Ion by Human Growth Hormone
title_full A Microcalorimetry Study of the Binding of Nickel Ion by Human Growth Hormone
title_fullStr A Microcalorimetry Study of the Binding of Nickel Ion by Human Growth Hormone
title_full_unstemmed A Microcalorimetry Study of the Binding of Nickel Ion by Human Growth Hormone
title_short A Microcalorimetry Study of the Binding of Nickel Ion by Human Growth Hormone
title_sort microcalorimetry study of the binding of nickel ion by human growth hormone
topic human growth hormone
nickel ion
metal binding
titration calorimetry
url http://www.ijcce.ac.ir/article_6397_916950c3c45b35ab9e7739e6a7bb308b.pdf
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