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Purification of soluble murine interleukin 5 (IL-5) receptor alpha expressed in Chinese hamster ovary cells and its action as an IL-5 antagonist.

Abstract：

:Recombinant soluble murine interleukin 5 receptor alpha (sIL-5R alpha) was expressed in Chinese hamster ovary cells and its biological activity was characterized. By using murine IL-5-coupled Sepharose, the single step purification method of the protein was established. The purified protein inhibited the murine IL-5-induced differentiation of BCL1 cells into immunoglobulin M-secreting cells in a dose-dependent manner. Moreover, it also inhibited murine IL-5-induced but not human IL-5-induced proliferation of TF-1 cells. These results indicated that sIL-5R alpha acted as an IL-5 antagonist and apparent species specificity of IL-5 action on murine cells was mediated, at least in part, by the alpha-chain of the IL-5 receptor.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Tsuruoka N,Yamashiro K,Tsujimoto M

doi

10.1006/abbi.1993.1571

subject

Has Abstract

pub_date

1993-11-15 00:00:00

pages

133-7

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(83)71571-7

journal_volume

307

pub_type

杂志文章

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