Thermodynamic study of the binding of calcium and magnesium ions with myelin basic protein using the extended solvation theory.
The interaction of myelin basic protein (MBP) from the bovine central nervous system with Ca2+ and Mg2+ ions, named as M2+, was studied by isothermal titration calorimetry at 27 degrees C in aqueous solution. The extended solvation model was used to reproduce the enthalpies of MBP+M2+ interactions. The solvation parameters recovered from the extended solvation model were attributed to the structural change of MBP due to the metal ion interaction. It was found that there is a set of two identical and noninteracting binding sites for Ca2+ and Mg2+ ions.
Behbehani
G Rezaei
GR
Chemistry Department, Imam Khomeini International University, Qazvin, Iran. grb402003@yahoo.com
Saboury
A A
AA
Divsalar
A
A
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002412:Cations; D002417:Cattle; D008274:Magnesium / Q000378:metabolism*; D008962:Models, Theoretical; D004676:Myelin Basic Protein / Q000378:metabolism*; D012995:Solubility; D013816:Thermodynamics
D002412:Cations; D004676:Myelin Basic Protein; D008274:Magnesium; D002118:Calcium