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用pH计和Cd离子选择电极测定了金属硫蛋白的加质子常数及其与Cd(Ⅱ)的络合常数,用改进的简化络合模型处理实验结果,得到了去金属硫蛋白(apo MT)中6类不同的加质子基团的数目及其加质子常数。对Cd(Ⅱ)滴定数据的计算表明,MT中两个结构域——α和β对Cd(Ⅱ)的络合常数相差约1000倍。从热力学定量描述了MT中两个结构域结合金属离子选择优先顺序。
The proton constant of metallothionein and its complexing constant with Cd (Ⅱ) were measured by pH meter and Cd ion selective electrode. The experimental results were obtained by the improved simplified complexation model, and the apo MT was obtained. In the six different types of proton-added groups and their proton-added protons. Calculations of Cd (II) titration data show that the two domains of MT - α and β have a difference of about 1000 times that of Cd (Ⅱ). Quantitative thermodynamics describes the order of preference for the binding of metal ions in the two domains of MT.