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.
MeSH terms
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Amidohydrolases
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Amino Acid Sequence
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Binding, Competitive
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Cells, Cultured
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Chromatography
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Chromatography, High Pressure Liquid
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Dinoprostone / biosynthesis
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Electrophoresis, Polyacrylamide Gel
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Fibroblasts / metabolism
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Glycosylation
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Humans
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Interleukin 1 Receptor Antagonist Protein
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Interleukin-1 / antagonists & inhibitors*
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Molecular Sequence Data
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Monocytes / metabolism*
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Peptide Fragments
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
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Proteins / isolation & purification*
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Proteins / metabolism
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Proteins / pharmacology
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Receptors, Immunologic / antagonists & inhibitors*
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Receptors, Immunologic / metabolism
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Receptors, Interleukin-1
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Recombinant Proteins / metabolism
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Recombinant Proteins / pharmacology
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Sialoglycoproteins*
Substances
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IL1RN protein, human
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Interleukin 1 Receptor Antagonist Protein
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Interleukin-1
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Peptide Fragments
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Proteins
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Receptors, Immunologic
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Receptors, Interleukin-1
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Recombinant Proteins
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Sialoglycoproteins
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Amidohydrolases
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
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Dinoprostone