A structure for the porcine TSH receptor
- 25 February 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 181 (2) , 218-222
- https://doi.org/10.1016/0014-5793(85)80263-5
Abstract
Affinity purified, detergent‐solubilised porcine TSH receptors have been crosslinked to a 125I‐labelled photoactive derivative of TSH and analysed by gel electrophoresis, gel filtration and sucrose density gradient centrifugation. Our studies suggest that the porcine TSH receptor is made up of a hydrophilic A subunit with an M r about 45000 linked to an amphiphilic B subunit (M rapprox. 25 000) by a disulphide bridge(s). The A subunit forms the binding site for TSH on the outside of the cell membrane. The B subunit appears to penetrate the membrane and form the site for interaction with adenylate cyclase either in the lipid bilayer or close to the cytoplasmic surface of the membrane.Keywords
This publication has 12 references indexed in Scilit:
- A structural comparison of guinea pig thyroid and fat TSH receptors by photoaffinity labellingFEBS Letters, 1984
- A water-soluble fragment of the thyroid-stimulating hormone receptor which binds both thyroid-stimulating hormone and thyroid-stimulating hormone receptor antibodiesJournal of Endocrinology, 1984
- Photo-affinity labelling of the thyrotropin receptorFEBS Letters, 1982
- Evidence that the porcine thyrotropin (TSH) receptor contains an essential disulphide bridgeMolecular and Cellular Endocrinology, 1982
- The interaction of graves' IgG with the thyrotrophin receptorFEBS Letters, 1981
- Biochemistry of major human histocompatibility antigensImmunology Today, 1980
- The role of hormone receptors and GTP-regulatory proteins in membrane transductionNature, 1980
- Time-dependent stabilisation of the TSH-TSH receptor complexFEBS Letters, 1980
- STUDIES ON THE BINDING ACTIVITY FOR THE LONG-ACTING THYROID STIMULATORJournal of Endocrinology, 1973
- A theory of gel filtration and its exeperimental verificationJournal of Chromatography A, 1964