Kabziński A K
University of Łódz, Faculty of Mathematic, Physics and Chemistry, Department of General and Inorganic Chemistry, Chromatography, Biochromatography and Environmental Analysis Laboratory, Narutowicza, 68 str., Poland.
Talanta. 1998 Jun;46(2):335-46.
The aim of this study was to present a new analytical method for the quantitative determination of metallothionein (MT) proteins in human body fluids and tissues, in order to determine the level of environmental and industrial exposure to heavy metals. For MT isolation, covalent affinity chromatography with thiol-disulphide inter-change (CAC-TDI) was applied. Fundamentals of indirect determination of the contents of metallothionein proteins were worked out through estimation of the quantities of metals bound with metallothionein protein and adsorbed on covalent affinity chromatography gel as on solid-phase extraction support during separating process. The (CAC-TDI) gel, specially prepared, was used as a solid phase extraction support (SPE) for preconcentration of Hg-thionein (Hg-Th), Cd-thionein (Cd-Th), Zn-thionein (Zn-Th) and Cu-thionein (Cu-Th) proteins and Hg, Cd, Zn and Cu bonded with MTs from water, human fluids such as: urine, human plasma, breast milk and tissues homogenates.
本研究的目的是提出一种新的分析方法，用于定量测定人体体液和组织中的金属硫蛋白（MT），以确定环境和工业中重金属的暴露水平。对于MT的分离，采用了具有硫醇-二硫键交换的共价亲和色谱法（CAC-TDI）。通过估算在分离过程中与金属硫蛋白结合并吸附在共价亲和色谱凝胶（作为固相萃取支持物）上的金属量，得出了间接测定金属硫蛋白含量的基本方法。特制的（CAC-TDI）凝胶用作固相萃取支持物（SPE），用于预富集汞硫蛋白（Hg-Th）、镉硫蛋白（Cd-Th）、锌硫蛋白（Zn-Th）和铜硫蛋白（Cu-Th）以及与MT结合的汞、镉、锌和铜，这些物质来自水、人体体液（如尿液、人血浆、母乳）和组织匀浆。
