Abstract：The performance of competing binding reactions between metal-ion group and human serum albumin(HSA) was investigated using affinity capillary electrophoresis (ACE) method. Based on the site binding model, a model about the interaction between [Zn2+, Cu2+] as the ligand and HSA as the receptor was established, a theoretical equation of competing binding reactions between multimetal-ions and macromolecule had been suggested, the binding parameters and dynamic mechanism were also measured and analyzed. The result showed that, the competitive combining reactions of metal-ion group [Zn2+, Cu2+ ] with HSA were reacted to form compounds Zn2+-HSA and Cu2+-HSA. Based on changes of the effective mobility, the mean apparent competition binding constant was determined through established theoretical equation by using non-linear fitting method, and the average apparent binding constant K[Zn2+-HSA]=(4.67±0.13)×104 L/mol, K[Cu2+-HSA]= (7.69±0.11)×104 L/mol. The binding reactions of Zn2+/Cu2+-HSA were equilibrium reactions, and that Cu2+ had antagonistic effect on Zn2+. Dosage-dependent effect existed among the peak height of compounds with the ligand strength of binding reactions and stability of compounds. This work has referential meaning for understanding deeply the transport mechanism of multimetal-ions with protein.
郭明,黄凤琴,李铭慧,刘敏. 金属离子组与人血清白蛋白的相互作用机制研究[J]. , 2014, 22(7): 892-902.
Ming GUO 2, 2, 2. Interaction Mechanism Research on Metal-ion Group Binding with Human Serum Albumin. , 2014, 22(7): 892-902.
