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  • Title: Effect of solubilization of porcine thyrotropin (TSH) receptor on TSH binding and on radio-receptor assay for anti-TSH receptor antibodies.
    Author: Watanabe Y, Tada H, Hidaka Y, Takano T, Amino N.
    Journal: Biochem Biophys Res Commun; 1998 Jul 09; 248(1):110-4. PubMed ID: 9675095.
    Abstract:
    The effect of solubilization of porcine thyrotropin receptor (TSHR) on TSH binding and on the radio-receptor assay for anti-TSHR antibodies was examined. After TSHR solubilization with 1% dodecylpolyethy-leneglycoether, TSH binding affinity was increased, from Kd = 1.15 nM to 0.45 nM, and TSH binding capacity was slightly increased, from 0.15 nM to 0.19 nM. With a particulate membrane suspension from thyroid cells, blocking of TSH binding to the membrane suspension by anti-thyrotropin receptor antibody was observed only for thyroid stimulation blocking antibody (TSBAb), not for thyroid-stimulating antibody (TSAb). After the solubilization of TSHR, both TSBAb and TSAb blocked TSH-binding to the solubilized TSHR. We speculate that TSAb interacts with the TSHR in the native conformation without interfering with TSH binding, and that after the solubilization, any anti-TSHR antibody interferes with TSH-binding due to the conformational change in TSHR. With these particulate thyroid cell membrane preparations, we can detect only TSBAb by the radio-receptor assay.
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