Purification of an endothelin receptor from human placenta |
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| Authors: | K Wada H Tabuchi R Ohba M Satoh Y Tachibana N Akiyama O Hiraoka A Asakura C Miyamoto Y Furuichi |
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| Institution: | Department of Molecular Genetics, Nippon Roche Research Center, Kamakura, Japan. |
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| Abstract: | 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. |
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