Section 41
Chapter 40,314

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

Steinkasserer, A.; Solari, R.; Mott, H.R.; Aplin, R.T.; Robinson, C.C.; Willis, A.C.; Sim, R.B.

Febs Letters 310(1): 63-65


ISSN/ISBN: 0014-5793
PMID: 1388125
DOI: 10.1016/0014-5793(92)81147-e
Accession: 040313855

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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.

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