Repository of Research and Investigative Information

Repository of Research and Investigative Information

Ilam University of Medical Sciences

Thermodynamic Studies on the Interaction of Nickel with Human Serum Albumin

Tue Jun 25 11:27:20 2024

(2003) Thermodynamic Studies on the Interaction of Nickel with Human Serum Albumin. Progress in Biochemistry and Biophysics. pp. 732-737. ISSN 10003282 (ISSN)

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The interaction of human serum albumin with divalent nickel ion was studied by equilibrium dialysis, isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC) and circular dichroism (CD) in 30 mmol/ L Tris buffer, pH = 7.0. There is a set of 8 identical binding sites for nickel binding on the protein at two temperatures of 300 K and 310 K. The cooperativity in the binding is observed at 310 K. The Hill coefficients at 300 K and 310 K are 0.97 and 1.25, respectively. The interaction between nickel ions and HSA is exothermic. A value of -36.5 kJ for enthalpy of interaction (1: 1 stoichiometry) was obtained. The secondary structure of HSA dose not show any change during the binding nickel ions process. However, the tertiary structure of the protein changes, which shows the existence of two natives like states.

Item Type: Article
Hosseini-Kishani, F.UNSPECIFIED
Rezaei-Tawirani, M.UNSPECIFIED
Keywords: Circular dichroism Differential scanning calorimetry Isothermal titration calorimetry Nickel Serum albumin human serum albumin article binding kinetics binding site calorimetry dialysis enthalpy human isotherm pH protein interaction protein secondary structure stoichiometry temperature thermodynamics titrimetry
Page Range: pp. 732-737
Journal or Publication Title: Progress in Biochemistry and Biophysics
Journal Index: Scopus
Volume: 30
Number: 5
ISSN: 10003282 (ISSN)
Depositing User: مهندس مهدی شریفی

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