Characterization of the guinea pig adipocyte thyrotropin receptor |
| |
| Authors: | S E Gennick C G Thomas S N Nayfeh |
| |
| Affiliation: | 1. Department of Biochemistry, The University of North Carolina, Chapel Hill, NC 27514 USA;2. Department of Surgery, The University of North Carolina, Chapel Hill, NC 27514 USA;1. Department of Internal Medicine, West Virginia University School of Medicine, Morgantown, West Virginia;2. Section of Endocrinology and Metabolism, Department of Internal Medicine, West Virginia University School of Medicine, Morgantown, West Virginia;1. Division of Endocrinology, Department of Pediatrics, The Warren Alpert Medical School of Brown University, Providence, Rhode Island;2. Section of Adult and Pediatric Endocrinology, Department of Medicine, The University of Chicago, Chicago, Illinois |
| |
| Abstract: | 125I-TSH binding to porcine thyroid and guinea pig fat resulted in curvilinear Scatchard plots with similar dissociation constants for the high and low affinity binding components. Antibodies from the sera of patients with Graves' disease inhibited binding to the high and low affinity binding components of both tissues. Covalent cross-linking of 125I-TSH to membranes from each tissue resulted in the specific labeling of two protein bands. The guinea pig fat receptor subunits have Mr values of 52,000 and 38,000, whereas the porcine thyroid receptor subunits have values of 46,000 & 35,000. The labeling of the receptor subunits was inhibited by preincubation with Graves' autoantibodies. Despite possessing a different subunit composition, the receptors from these tissues exhibit similar affinity for TSH and share similar antigenic determinants for Graves' autoantibodies. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
