Interleukin-1 receptor antagonist activity of a human interleukin-1 inhibitor.
摘要：
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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关键词：
Humans Fibroblasts Monocytes Cells, Cultured Amidohydrolases Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Proteins Dinoprostone Recombinant Proteins Receptors, Immunologic
DOI：
10.1038/343336a0
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年份：
1990
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