Abstract
Three interleukin-1 inhibitors have been purified to homogeneity from medium conditioned by human monocytes. Partial sequence analysis and digestion with N-glycanase indicate that these are glycosylation forms of a single protein. The protein binds to the interleukin-1 receptor but has no interleukin-1-like activity, even at very high concentrations, and is therefore a pure receptor antagonist.
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Hannum, C., Wilcox, C., Arend , W. et al. Interleukin-1 receptor antagonist activity of a human interleukin-1 inhibitor. Nature 343, 336–340 (1990). https://doi.org/10.1038/343336a0
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DOI: https://doi.org/10.1038/343336a0
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