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Human interleukin-1 receptor antagonist. High yield expression in E. coli and examination of cysteine residues.

Abstract:
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.
Publication status:
Published

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Role:
Author
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Journal:
FEBS letters
Volume:
310
Issue:
1
Pages:
63-65
Publication date:
1992-09-05
DOI:
EISSN:
1873-3468
ISSN:
0014-5793
URN:
uuid:8d4863cf-5d83-44ab-b4f0-a1fe70429c9f
Source identifiers:
59798
Local pid:
pubs:59798

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