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Further characterization of the low and high affinity binding components of the thyrotropin receptor

Journal Article · · Biochem. Biophys. Res. Commun.; (United States)
Following cross-linking with disuccinimdiyl suberate and analysis by SDS-PAGE and autoradiography, both the high- and low-affinity TSH binding components exhibited two similar /sup 125/I-TSH-labeled bands, with Mr values of 80,000 and 68,000. IgG fractions from patients with Graves' disease inhibited /sup 125/I-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.
Research Organization:
Univ. of North Carolina, Chapel Hill
OSTI ID:
5009167
Journal Information:
Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 137:1; ISSN BBRCA
Country of Publication:
United States
Language:
English