Interleukin-1 receptor antagonist activity of a human interleukin-1 inhibitor.

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.

journal_name

Nature

journal_title

Nature

authors

Hannum CH,Wilcox CJ,Arend WP,Joslin FG,Dripps DJ,Heimdal PL,Armes LG,Sommer A,Eisenberg SP,Thompson RC

doi

10.1038/343336a0

subject

Has Abstract

pub_date

1990-01-25 00:00:00

pages

336-40

issue

6256

eissn

0028-0836

issn

1476-4687

journal_volume

343

pub_type

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