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A structure for the porcine TSH receptor
Author(s) -
Kajita Yoshihiro,
Rickards Carole R.,
Buckland Paul R.,
Howells Roger D.,
Smith Bernard Rees
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80263-5
Subject(s) - protein subunit , chemistry , receptor , membrane , centrifugation , cytoplasm , octyl glucoside , biochemistry , lipid bilayer , size exclusion chromatography , cyclase , gel electrophoresis , chromatography , enzyme , gene
Affinity purified, detergent‐solubilised porcine TSH receptors have been crosslinked to a 125 I‐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 r approx. 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.