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- W2024532615 abstract "Affinity chromatography of crude human urinary proteins on either human recombinant interleukin-6 (rIL-6) or human recombinant interferon-γ (rIFN-γ) or anti IFN-γ receptor (IFN-γ-R) monoclonal antibodies (McAb) yielded the two respective soluble receptors in significant amounts. A single sequence of 30 amino acid residues was obtained by N-terminal microsequencing of the protein peak purified in tandem by affinity chromatography on an IL-6 column and reveresed-phase high-performance liquid chromatography. This sequence was identical with the predicted N-terminal sequence of IL-6-R as previously reported. The purified IL-6-R retained its biological activity. It was used for the preparation of specific anti IL-6-R monoclonal antibodies. Analysis of the eluted proteins from both IFN-γ and anti IFN-γ-R columns by inhibition of solid-phase radioimmunoassay, enzyme-linked immunosorbent assay, sodium dodecyl sulphate—polyacrylamide gel electrophoresis and Western blotting proved the existence of soluble IFN-γ-R in normal urine. This finding together with the already known presence of soluble TNF receptors and a soluble IL-2 receptors found both in plasma and in urine indicates that release of soluble cytokine receptors into body fluids is a general phenomenon which occurs under normal physiological conditions." @default.
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- W2024532615 title "Purification of soluble cytokine receptors from normal human urine by ligand-affinity and immunoaffinity chromatography" @default.
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- W2024532615 doi "https://doi.org/10.1016/s0021-9673(01)93767-7" @default.
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