Evidence that the porcine thyrotropin (TSH) receptor contains an essential disulphide bridge.
The effects of reducing agents on membrane bound and detergent solubilised porcine TSH receptors have been investigated. Both 2-mercaptoethanol and dithiothreitol appeared to inhibit the TSH-binding activity by a direct effect on the TSH receptor itself and Scatchard analysis suggested that this was primarily due to an alteration in TSH-binding capacity. In addition, some binding activity could be recovered by reoxidation of reduced receptor preparations. These results suggest therefore that the porcine TSH receptor contains an essential disulphide bridge.
D000818:Animals; D003902:Detergents / Q000494:pharmacology; D004220:Disulfides / Q000032:analysis*; D004229:Dithiothreitol / Q000494:pharmacology; D008623:Mercaptoethanol / Q000494:pharmacology; D010084:Oxidation-Reduction; D011956:Receptors, Cell Surface / Q000032:analysis*; D011989:Receptors, Thyrotropin; D013552:Swine
D003902:Detergents; D004220:Disulfides; D011956:Receptors, Cell Surface; D011989:Receptors, Thyrotropin; D008623:Mercaptoethanol; D004229:Dithiothreitol