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Various glutathione S-transferase fusion proteins have been constructed, which allow the isolation of cell surface proteins by affinity chromatography on glutathione-agarose. The cytoplasmic domains of the polypeptides were fused to the N terminus of the Escherichia coli glutathione S-transferase protein. Different kinds of covalent linkages of the fusion polypeptides to the glutathione S-transferase protein were used: Cys-Cys, Cys-Gly, Cys-Gly-Cys, Cys-Arg. The fusion proteins were readily expressed in E. coli and were readily purified to homogeneity.[The atomic-coupled electron-nuclear double resonance spectroscopic study of polychlorinated dibenzo-p-dioxins].
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