Study of the binding equilibrium between Zn(II) and HSA by capillary electrophoresis-inductively coupled plasma optical emission spectrometry |
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Authors: | Deng Biyang Wang Yingzi Zhu Pingchuan Xu Xiangshu Ning Xi |
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Institution: | Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources (Ministry of Education of China), College of Chemistry and Chemical Engineering, Guangxi Normal University, Guilin 541004, China |
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Abstract: | A new method has been developed for following the interaction between zinc ion and human serum albumin (HSA) by capillary electrophoresis-inductively coupled plasma optical emission spectrometry. Under optimized experimental conditions, the detection limit (3σ) for free Zn2+ ion was found to be 1.34 μM by running 11 replicates of the reagent blank. The RSD was less than 3% and the recovery was more than 98.13%. The linear range of zinc ion concentration was between 5.1 μM and 0.3 M. The measured Zn(II)-HSA combination values of n1 and K1 for primary binding of Zn2+ to HSA were 1.09 and 2.29 × 105 L mol−1, respectively. The measured values of n2 and K2 for the non-specific binding of Zn2+ to HSA were 8.96 and 6.65 × 103 L mol−1, respectively. This new method allows rapid analysis of a small amount of sample, simple operation, while avoiding long periods of dialysis and eliminating interference from other metal ions. This method provides a reliable and convenient new way for studying interactions between metal ions and biomolecules. |
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Keywords: | Binding interaction Capillary electrophoresis Inductively coupled plasma optical emission spectroscopy Zinc Human serum albumin |
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