A thermodynamic study on the binding of calcium ion with myelin basic protein
A thermodynamic study on the binding of calcium ion with myelin basic protein
复制标题
DOI：
10.1007/s10953-007-9181-y
复制
发表时间：
2007-10-01
影响因子：
1.2
通讯作者：
Baghery, A. Fallah
中科院分区：
文献类型：
--
作者：
Behbehani, G. Rezaei;Saboury, A. A.;Baghery, A. Fallah
用27℃恒温滴定热法研究了牛中枢神经系统髓鞘碱性蛋白(MBP)与二价钙离子的相互作用。扩展溶剂化模型被用来再现整个Ca~(2+)浓度范围内的Ca~(2+)-MBP相互作用的焓。从溶剂化模型恢复的溶剂化参数归因于金属离子相互作用引起的MBP结构的变化。研究发现，钙离子存在两个相同且不相互作用的结合部位。缔合平衡常数为0.021µmol.dm(-3)。摩尔结合热为Delta H=-15.10kJ.mol(-1)。
The interaction of myelin basic protein (MBP) from the bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27 degrees C in aqueous solution. The extended solvation model was used to reproduce the enthalpies of Ca2+-MBP interaction over the whole range of Ca2+ concentrations. The solvation parameters recovered from the 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 non-interacting binding sites for Ca2+ ions. The association equilibrium constant is 0.021 mu mol.dm(-3). The molar enthalpy of binding is Delta H=-15.10 kJ.mol(-1).