Van Hulle M, De Cremer K, Cornelis R
Laboratory for Analytical Chemistry, Ghent University, Belgium.
Fresenius J Anal Chem. 2000 Sep-Oct;368(2-3):293-6. doi: 10.1007/s002160000430.
The chemical speciation of indium in serum was studied. Ultrafiltration was used to investigate the influence of several buffer systems on the binding characteristics of indium in serum and to study the association of indium with transferrin and albumin. This was performed by means of batch incubation experiments with a 114mIn tracer. Different buffer systems were investigated. A series of bicarbonate, Tris:HCl and HEPES buffers were found to fit for this purpose. Phosphate buffer was not suitable, as it is capable of disrupting the binding between indium and transferrin. Batch ultrafiltration experiments with 114mIn incubated solutions of transferrin and albumin showed that both proteins are capable of binding indium to a high degree. Three chromatographic techniques (SEC, AEC, AC) were used to study the different chemically active species of indium in serum. It is concluded that next to transferrin, albumin is also responsible for the binding and transport of indium in serum.
研究了血清中铟的化学形态。采用超滤法研究了几种缓冲体系对血清中铟结合特性的影响，并研究了铟与转铁蛋白和白蛋白的结合情况。这是通过使用114mIn示踪剂进行批量孵育实验来完成的。研究了不同的缓冲体系。发现一系列碳酸氢盐、Tris:HCl和HEPES缓冲液适用于此目的。磷酸盐缓冲液不合适，因为它能够破坏铟与转铁蛋白之间的结合。用114mIn孵育转铁蛋白和白蛋白溶液进行的批量超滤实验表明，这两种蛋白质都能够高度结合铟。使用三种色谱技术（SEC、AEC、AC）研究血清中铟的不同化学活性物种。得出的结论是，除了转铁蛋白外，白蛋白也负责血清中铟的结合和运输。
