Published May 29, 1986
| Version v1
Journal article
Further characterization of the low and high affinity binding components of the thyrotropin receptor
Description
Following cross-linking with disuccinimdiyl suberate and analysis by SDS-PAGE and autoradiography, both the high- and low-affinity TSH binding components exhibited two similar 125I-TSH-labeled bands, with Mr values of 80,000 and 68,000. IgG fractions from patients with Graves' disease inhibited 125I-TSH binding to both components, while normal IgG had no effect. Although not entirely conclusive, these results suggest that the high- and low-affinity components share similar subunit composition and antigenic determinants
Additional details
Publishing Information
- Journal Title
- Biochem. Biophys. Res. Commun.
- Journal Volume
- 137
- Journal Issue
- 1
- Series
- Biochem. Biophys. Res. Commun.
- Journal Page Range
- 61-68
- ISSN
- 0006-291X
- CODEN
- BBRCA
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 18018487
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Resource subtype / Literary indicator
- Numerical Data
- Descriptors DEI
- AUTORADIOGRAPHY; BIOCHEMICAL REACTION KINETICS; DIAGNOSIS; ENDOCRINE DISEASES; EXPERIMENTAL DATA; IODINE 125; LABELLED COMPOUNDS; PATIENTS; RADIORECEPTOR ASSAY; RECEPTORS; TRACER TECHNIQUES; TSH
- Descriptors DEC
- BETA DECAY RADIOISOTOPES; DATA; DAYS LIVING RADIOISOTOPES; DISEASES; ELECTRON CAPTURE RADIOISOTOPES; HORMONES; INFORMATION; INTERMEDIATE MASS NUCLEI; INTERNAL CONVERSION RADIOISOTO; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; KINETICS; NUCLEI; NUMERICAL DATA; ODD-EVEN NUCLEI; PEPTIDE HORMONES; PITUITARY HORMONES; RADIOISOTOPES; REACTION KINETICS