PRODUCTION AND LIGAND-BINDING CHARACTERISTICS OF THE SOLUBLE FORM OF MURINE ERYTHROPOIETIN RECEPTOR

被引:55
作者
NAGAO, M [1 ]
MASUDA, S [1 ]
ABE, S [1 ]
UEDA, M [1 ]
SASAKI, R [1 ]
机构
[1] SNOW BRAND MILK PROD CO LTD, LIFE SCI RES INST, TOCHIGI 32905, JAPAN
关键词
D O I
10.1016/0006-291X(92)91139-H
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. © 1992.
引用
收藏
页码:888 / 897
页数:10
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