| Literature DB >> 1388125 |
A Steinkasserer1, R Solari, H R Mott, R T Aplin, C C Robinson, A C Willis, R B Sim.
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.Entities:
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Year: 1992 PMID： 1388125 DOI： 10.1016/0014-5793(92)81147-e
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124