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  • Title: Purification of an endothelin receptor from human placenta.
    Author: Wada K, Tabuchi H, Ohba R, Satoh M, Tachibana Y, Akiyama N, Hiraoka O, Asakura A, Miyamoto C, Furuichi Y.
    Journal: Biochem Biophys Res Commun; 1990 Feb 28; 167(1):251-7. PubMed ID: 2155613.
    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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