Study of the binding equilibrium between Zn(II) and HSA by capillary electrophoresis–inductively coupled plasma optical emission spectrometry
| Autor: | Pingchuan Zhu, Biyang Deng, Xiangshu Xu, Yingzi Wang, Xi Ning |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Detection limit
Binding Sites Metal ions in aqueous solution Analytical chemistry Electrophoresis Capillary chemistry.chemical_element Zinc Human serum albumin Mass spectrometry Biochemistry Mass Spectrometry Analytical Chemistry Ion Kinetics Capillary electrophoresis chemistry medicine Humans Environmental Chemistry Inductively coupled plasma Serum Albumin Spectroscopy Protein Binding medicine.drug |
| Zdroj: | Analytica Chimica Acta. 683:58-62 |
| ISSN: | 0003-2670 |
| DOI: | 10.1016/j.aca.2010.10.018 |
| Popis: | 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 Zn(2+) 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 0.3M. The measured Zn(II)-HSA combination values of n(1) and K(1) for primary binding of Zn(2+) to HSA were 1.09 and 2.29×10(5) L mol(-1), respectively. The measured values of n(2) and K(2) for the non-specific binding of Zn(2+) to HSA were 8.96 and 6.65×10(3) 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. |
| Databáze: | OpenAIRE |
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