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.
Anal Chim Acta. 2010 Dec 17;683(1):58-62. doi: 10.1016/j.aca.2010.10.018. Epub 2010 Oct 19.
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.
一种新的方法已经被开发出来，用于通过毛细管电泳-电感耦合等离子体发射光谱法来跟踪锌离子与人血清白蛋白（HSA）之间的相互作用。在优化的实验条件下，通过运行 11 次试剂空白的重复实验，发现游离 Zn(2+)离子的检测限（3σ）为 1.34 μM。相对标准偏差（RSD）小于 3%，回收率大于 98.13%。锌离子浓度的线性范围在 5.1 μM 和 0.3M 之间。测定的 Zn(II)-HSA 结合值 n(1)和 K(1)分别为 1.09 和 2.29×10(5) L mol(-1)，用于 Zn(2+)与 HSA 的初级结合。测定的 Zn(II)-HSA 非特异性结合值 n(2)和 K(2)分别为 8.96 和 6.65×10(3) L mol(-1)。这种新方法允许对少量样品进行快速分析，操作简单，同时避免了长时间的透析和消除了其他金属离子的干扰。该方法为研究金属离子与生物分子之间的相互作用提供了一种可靠、方便的新途径。
