PURIFICATION OF AN ENDOTHELIN RECEPTOR FROM HUMAN PLACENTA

被引：81

作者：

WADA, K ^{[1
]}

TABUCHI, H ^{[1
]}

OHBA, R ^{[1
]}

SATOH, M ^{[1
]}

TACHIBANA, Y ^{[1
]}

AKIYAMA, N ^{[1
]}

HIRAOKA, O ^{[1
]}

ASAKURA, A ^{[1
]}

MIYAMOTO, C ^{[1
]}

FURUICHI, Y ^{[1
]}

机构：

[1] NIPPON ROCHE RES CTR,DEPT MOLEC GENET,KAMAKURA,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 167卷 / 01期

关键词：

D O I：

10.1016/0006-291X(90)91758-K

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：

We have identified an endothelin (ET) binding protein on the membranes of human placenta and purified it to homogeneity. It is a polypeptide with an apparent Mol. Wt. of 40,000 and is a major protein to be labeled by cross-linking with either 125I-ET-1, -2, or -3. Binding studies with Scatchard analysis indicated the presence of a single class, high-affinity binding site with Kds of 57 pM, 480 pM and 40 nM for 125I-labeled ET-1, ET-2 and ET-3, respectively. These results suggest that the 40K protein is a major ET receptor in placenta and, most likely, can bind differentially to ET-1, ET-2 and ET-3. © 1990.

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页码：251 / 257

页数：7

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