A thermodynamic study on the interaction of nickel ion with myelin basic protein by isothermal titration calorimetry

2009 ◽  
Vol 101 (1) ◽  
pp. 379-384 ◽  
Author(s):  
G. Rezaei Behbehani ◽  
A. A. Saboury ◽  
L. Barzegar ◽  
O. Zarean ◽  
J. Abedini ◽  
...  
2011 ◽  
Vol 110-116 ◽  
pp. 1963-1965
Author(s):  
M. Mirzaie ◽  
G. Rezaei Behbehani

The interaction of myelin basic protein with Nickel ions was studied by Isothermal Titration Calorimetry (ITC) at in tris buffer, pH=7. The enthalpies of MBP+Ni2+interaction are reported and analysed in term of the new solvation theory. It was found that MBP has three identical and cooperative binding sites for Ni2+ions. The dissociation equilibrium constant and the molar enthalpy of binding are 75.015 µM, -14.815 kJmol-1. The binding parameters recovered from the new equation, attributed to the structural change of MBP and its biological activity due to metal ion interaction. The binding of nickel ions cause some changes in stability of MBP at low and high Ni2+concentrations.


2017 ◽  
Vol 62 (2) ◽  
pp. 729-737 ◽  
Author(s):  
Paulo F. R. Ortega ◽  
João Paulo C. Trigueiro ◽  
Merly R. Santos ◽  
Ângelo M. L. Denadai ◽  
Luiz Carlos A. Oliveira ◽  
...  

2007 ◽  
Vol 36 (10) ◽  
pp. 1311-1320 ◽  
Author(s):  
G. Rezaei Behbehani ◽  
A. A. Saboury ◽  
A. Fallah Baghery

2018 ◽  
Vol 136 (4) ◽  
pp. 1701-1709 ◽  
Author(s):  
Norma Rodríguez-Laguna ◽  
Luis Ignacio Reyes-García ◽  
Raúl Pacheco-Gómez ◽  
Raúl Flores ◽  
Alberto Rojas-Hernández ◽  
...  

2010 ◽  
Vol 28 (5) ◽  
pp. 713-718 ◽  
Author(s):  
G. Rezaei Behbehani ◽  
A. A. Saboury ◽  
O. Zarean ◽  
L. Barzegar ◽  
S. Ghamamy

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