CEA, CNRS, Aix-Marseille Université, UMR 7265 Biologie Végétale et Microbiologie Environnementales, Laboratoire des Interactions Protéine Métal, 13108 Saint-Paul-lez-Durance, France.
Doctor-on-a-Chip Laboratory, Electronic and Computer Engineering, College of Engineering, Design and Physical Sciences, Brunel University, Uxbridge, Middlesex UB8 3PH, UK.
Dalton Trans. 2017 Jan 31;46(5):1389-1396. doi: 10.1039/c6dt04336d.
Capillary electrophoresis coupled with an inductively coupled plasma mass spectrometer was applied for the first time to determine the binding constant of human transferrin (Tf) for tetravalent plutonium. The experiments were carried out in a buffer 2-(N-morpholino)ethanesulfonic acid (MES) at pH 6, 0.1 M NaCl and at a temperature of 25 °C. The nitrilotriacetate anion (NTA) used in this study prevents the hydrolysis of plutonium and is an ideal competitor with Tf for Pu, both ligands sharing comparable binding strength. The separation revealed unambiguous two peaks associated with the complex Pu(NTA) used as the initial species and with Pu-transferrin. Two series of independent experiments were conducted and gave the first stepwise conditional bicarbonate-free Pu-transferrin binding constant of . In the absence of bicarbonate the affinity of transferrin for plutonium at pH 6 is about 10 times stronger than that of iron at pH 6.7 .
毛细管电泳与电感耦合等离子体质谱联用首次被用于测定人转铁蛋白（Tf）与四价钚的结合常数。实验在 pH 值为 6、0.1 M NaCl 的 2-（N-吗啉基）乙磺酸（MES）缓冲液中，于 25°C 下进行。本研究中使用的氮三乙酸根阴离子（NTA）可防止钚水解，且是 Tf 与 Pu 的理想竞争配体，两种配体具有相当的结合强度。分离结果显示出与 Pu（NTA）初始物种和 Pu-转铁蛋白相关的两个明确的双峰。进行了两组独立的实验，得到了第一个无碳酸氢盐条件下的 Pu-转铁蛋白分步结合常数为 。在无碳酸氢盐的情况下，pH 值为 6 时转铁蛋白对钚的亲和力比 pH 值为 6.7 时铁的亲和力强约 10 倍。
