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Author Ji, T. H.
Source United States Department of Energy Office of Scientific and Technical Information
Content type Text
Language English
Subject Keyword RADIOLOGY AND NUCLEAR MEDICINE ♦ BASIC BIOLOGICAL SCIENCES ♦ FSH ♦ CROSS-LINKING ♦ RADIORECEPTOR ASSAY ♦ RECEPTORS ♦ ELECTROPHORESIS ♦ IODINE 125 ♦ MOLECULAR WEIGHT ♦ POLYETHYLENE GLYCOLS ♦ SOLUBILITY ♦ SWINE ♦ ALCOHOLS ♦ ANIMALS ♦ BETA DECAY RADIOISOTOPES ♦ CHEMICAL REACTIONS ♦ DAYS LIVING RADIOISOTOPES ♦ DOMESTIC ANIMALS ♦ ELECTRON CAPTURE RADIOISOTOPES ♦ GLYCOLS ♦ GONADOTROPINS ♦ HORMONES ♦ HYDROXY COMPOUNDS ♦ INTERMEDIATE MASS NUCLEI ♦ IODINE ISOTOPES ♦ ISOTOPE APPLICATIONS ♦ ISOTOPES ♦ MAMMALS ♦ NUCLEI ♦ ODD-EVEN NUCLEI ♦ ORGANIC COMPOUNDS ♦ ORGANIC POLYMERS ♦ PEPTIDE HORMONES ♦ PITUITARY HORMONES ♦ POLYMERIZATION ♦ POLYMERS ♦ RADIOISOTOPES ♦ TRACER TECHNIQUES ♦ VERTEBRATES 550601* -- Medicine-- Unsealed Radionuclides in Diagnostics ♦ BiochemistryTracer Techniques
Abstract Both of the alpha and beta subunits of intact human follitropin (FSH) were radioiodinated with SVI-sodium iodide and chloramine-T and could be resolved on sodium dodecyl sulfate-polyacrylamide gels. Radioiodinated FSH was affinity-cross-linked with a cleavable (nondisulfide) homobifunctional reagent to its membrane receptor on the porcine granulosa cell surface as well as to a Triton X-100-solubilized form of the receptor. Cross-linked samples revealed three additional bands of slower electrophoretic mobility, corresponding to 65, 83, and 117 kDa, in addition to the hormone bands. The hormone alpha beta dimer band corresponded to 43 kDa. Formation of the three bands requires the SVI-hormone to bind specifically to the receptor with subsequent cross-linking. Binding was prevented by an excess of the native hormone but not by other hormones. A monofunctional analog of the cross-linking reagent failed to produce the three bands. Reagent concentration-dependent cross-linking revealed that their formation was sequential; smaller complexes formed first and then larger ones. When gels of cross-linked complexes were treated to cleave covalent cross-links and then electrophoresed in a second dimension, 18-, 22-, and 34-kDa components were released, in addition to the alpha and beta subunits of the hormone.
Educational Use Research
Learning Resource Type Article
Publisher Date 1985-10-15
Publisher Place United States
Journal J. Biol. Chem.
Volume Number 23
Organization Univ. of Wyoming, Laramie


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