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The human IL-1 receptor antagonist (IL-1ra) was produced in a high yield E. coli expression system, and was purified in a rapid two-step purification. This recombinant IL-1ra molecule possessed full binding activity to the IL-1 receptor (type I) and totally inhibited IL-1-induced PGE2 production by human dermal fibroblasts. Radioalkylation and analysis of V8-derived IL-1ra peptides indicate that the four cysteines present in the IL-1ra are not disulphide-linked.


Journal article



Publication Date





63 - 65


Amino Acid Sequence, Base Sequence, Binding, Competitive, Cloning, Molecular, Cysteine, Dinoprostone, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Humans, Interleukin 1 Receptor Antagonist Protein, Interleukin-1, Molecular Sequence Data, Oligonucleotides, Proteins, Receptors, Immunologic, Receptors, Interleukin-1, Recombinant Proteins, Sialoglycoproteins