Structure of the porcine thyrotropin receptor: a 200 kilodalton glycoprotein heterocomplex
- 1 January 1985
- journal article
- research article
- Published by Springer Nature in Cellular and Molecular Life Sciences
- Vol. 41 (1) , 18-23
- https://doi.org/10.1007/bf02005855
Abstract
We have determined that the porcine thyroidal TSH receptor is a glycoprotein heterotetramer composed of two Mr ∼ 35,000 (ɛ) covalently linked subunits which interact noncovalently with two copies of δ (Mr 66,000) chains.This publication has 42 references indexed in Scilit:
- 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
- “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein AAnalytical Biochemistry, 1981
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- SOLUBILIZATION AND PARTIAL CHARACTERIZATION OF HUMAN AND PORCINE THYROTROPHIN RECEPTORSJournal of Endocrinology, 1978
- High resolution two-dimensional electrophoresis of basic as well as acidic proteinsCell, 1977
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONSAnnals of the New York Academy of Sciences, 1949