title: Properties of thyrotropin receptor on cloned hybrid human thyroid cells.
abstract: Purification of the thyrotropin (TSH) binding sites from cloned human thyroid cells (GEJ) was performed after biosynthetic labelling of the cells, affinity chromatography on a human TSH-sepharose column and polyacrylamide gel electrophoresis in sodium dodecyl sulphate (PAGE-SDS). The relative molecular mass (Mr) of the GEJ cell TSH receptor (TSH-R) was approximately 48,000. This was confirmed by cross-linking [125I]TSH to GEJ binding sites with two homobifunctional agents: dimethyl suberimidate and disuccinimidyl suberate. Moreover, the absence of a dithiothreitol effect demonstrated that the TSH binding site on GEJ cells is formed by a single chain lacking disulphide bonds.
mesh_terms: D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D002846:Chromatography, Affinity; D002999:Clone Cells; D006801:Humans; D011989:Receptors, Thyrotropin / Q000302:isolation & purification / Q000378:metabolism*; D013961:Thyroid Gland / Q000378:metabolism*
chemical_list: D011989:Receptors, Thyrotropin