Further characterization of the low and high affinity binding components of the thyrotropin receptor.
Following cross-linking with disuccinimidyl suberate and analysis by SDS-PAGE and autoradiography, both the high- and low-affinity TSH binding components exhibited two similar 125I-TSH-labeled bands, with Mr values of 80,000 and 68,000. IgG fractions from patients with Graves' disease inhibited 125I-TSH binding to both components, while normal IgG had no effect. Although not entirely conclusive, these results suggest that the high- and low-affinity components share similar subunit composition and antigenic determinants.
D000818:Animals; D000918:Antibody Specificity; D001323:Autoantibodies / Q000276:immunology; D003208:Concanavalin A / Q000378:metabolism; D006111:Graves Disease / Q000276:immunology; D006801:Humans; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D008970:Molecular Weight; D011956:Receptors, Cell Surface / Q000276:immunology / Q000378:metabolism*; D011989:Receptors, Thyrotropin; D013329:Structure-Activity Relationship; D013552:Swine; D013972:Thyrotropin / Q000378:metabolism*
D001323:Autoantibodies; D046911:Macromolecular Substances; D011956:Receptors, Cell Surface; D011989:Receptors, Thyrotropin; D003208:Concanavalin A; D013972:Thyrotropin