PMID: 7538754May 15, 1995Paper

Immunochemical characterization of two thyroid-stimulating hormone beta-subunit epitopes

The Biochemical Journal
W D FairlieM T Hearn

Abstract

The epitopes of human thyroid-stimulating hormone (hTSH) recognized by two murine monoclonal antibodies (MAbs), designated MAb 279 and MAb 299, have been characterized. These MAbs are highly specific for the beta-subunit of TSH. The epitope recognized by MAb 279 appears to be completely conserved between bovine and human TSH and partially conserved in the porcine species. The TSH beta-subunit epitope recognized by MAb 299 is only partially conserved between the human, bovine and porcine species. Both MAbs are capable of inhibiting the binding of TSH to its receptor in a TSH radioreceptor assay, indicating that the epitopes either coincide or are located close to the TSH beta-subunit receptor-binding sites. The carbohydrate moieties of the TSH beta-subunit appear to play little or no role in the epitope recognition by MAb 279 or MAb 299 while the integrity of the disulphide bonds are essential. The epitopic recognition may also involve lysine residues, as determined by the immunoreactivity with both MAbs following citraconylation of TSH. In addition, the amino acid sequence region between residues bTSH beta 34-44 could be excised by trypsin digestion of bovine TSH beta (bTSH beta) without eliminating epitopic recognition by eith...Continue Reading

Citations

Oct 12, 1999·The Journal of Peptide Research : Official Journal of the American Peptide Society·P T GommeM T Hearn
Dec 24, 2005·Rapid Communications in Mass Spectrometry : RCM·Willy MorelleJean-Claude Michalski
Mar 17, 1999·Journal of Biochemical and Biophysical Methods·P T GommeM T Hearn

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