Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochem Biophys Res Commun. 1992 Oct 30;188(2):888-97.

Production and ligand-binding characteristics of the soluble form of murine erythropoietin receptor.

Author information

1
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.

Abstract

A recombinant soluble form (sEPO-R) of erythropoietin (EPO) receptor (EPO-R) was produced by Chinese hamster ovary cells and isolated in high yield with the EPO-fixed gel. Ligand binding assays were done using three methods; precipitation of sEPO-R radiolabeled EPO complex and competition of sEPO-R for the binding of radiolabeled EPO with the cellular EPO-R. The results showed a Kd of 17 nM which was much lower than those for cellular EPO-R. One N-glycosylation site exists in sEPO-R but the glycosylation did not affect the binding affinity to EPO. A complex with a molecular size that corresponded to a 1:1 complex of EPO and sEPO-R was detected.

PMID:
1445329
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center