Sestáková I, Mader P
J. Heyrovský Institute of Physical Chemistry, Academy of Sciences of the Czech Republic, Prague.
Cell Mol Biol (Noisy-le-grand). 2000 Mar;46(2):257-67.
Rabbit liver Cd-metallothionein (CdMT) and Cd-complex of synthetically prepared pentapeptide (gamma-Glu-Cys)2-Gly were studied as examples of animal and plant metallothioneins. Using hanging mercury electrode, cathodic stripping voltammetry after adsorptive accumulation of the Cd(II)-SR complex at different potentials, is suitable for estimating changes occurring in metal coordination due to the presence of metal ions such as Zn2+, Cu2+, Hg2+ or excessive Cd2+. Conditions under which similar behaviour can be observed for both CdMT and Cd-pentapeptide complex are specified. On carbon electrodes, detailed study of reduction processes of Cd(II)-SR complexes is prevented by occurrence of a large catalytic current; oxidation processes are more suitable for study at these electrodes. Carbon composite paste electrode (10% SiO2) allows deposition of Cd(II)-SR complex during its reduction, as was demonstrated with Cd-cysteine, CdMT or Cd-pentapeptide complex. After deposition, oxidation peak of the uncomplexed Cd2+ ions and one or two oxidation peaks corresponding to a formation of the RS-Cd(II) complex are observed. Also, similarly as on Hg electrode, it was observed that excessive Cd2+ or Zn2+ ions influence oxidation peaks of the RS-Cd(II) complex formation. Combination of measurements on mercury electrode and composite paste electrode is recommended for studies of metallothionein interactions with metal ions or other metal complexes.
以兔肝镉金属硫蛋白(CdMT)和人工合成的五肽(γ-谷氨酰-半胱氨酸)2-甘氨酸的镉配合物作为动植物金属硫蛋白的实例进行了研究。使用悬汞电极,在不同电位下吸附积累Cd(II)-SR配合物后进行阴极溶出伏安法,适用于评估由于存在Zn2+、Cu2+、Hg2+或过量Cd2+等金属离子而导致的金属配位变化。确定了CdMT和镉五肽配合物都能观察到类似行为的条件。在碳电极上,Cd(II)-SR配合物还原过程的详细研究因出现大的催化电流而受阻;氧化过程更适合在这些电极上进行研究。碳复合糊电极(10%SiO2)在Cd(II)-SR配合物还原过程中允许其沉积,Cd-半胱氨酸、CdMT或镉五肽配合物的情况已得到证明。沉积后,观察到未络合的Cd2+离子的氧化峰以及对应于RS-Cd(II)配合物形成的一个或两个氧化峰。同样,与在汞电极上一样,观察到过量的Cd2+或Zn2+离子会影响RS-Cd(II)配合物形成的氧化峰。建议结合汞电极和复合糊电极的测量来研究金属硫蛋白与金属离子或其他金属配合物的相互作用。