Detection of TRH extended peptides in rat hypothalamus using an antibody raised to pGluHisProGlyLys.
An antibody was raised to the synthetic pentapeptide pGluHisProGlyLys which, in radioimmunoassay (RIA), could detect the pentapeptide at a level of 10 fmole per tube and exhibited less than 0.5 per cent cross reactivity with a series of related peptides. The RIA was used to demonstrate the presence of C-terminally extended forms of thyrotropin releasing hormone (TRH) in rat hypothalamus. After extraction, the endogenous peptides were resolved by gel exclusion chromatography and TRH-extended peptides were revealed by trypsin digestion to release the pentapeptide. The TRH extended peptides occurred in substantial quantity, approximately 11 pmoles/g, indicating that only partial processing of the gene duplicated prohormone takes place.
D000818:Animals; D000906:Antibodies / Q000276:immunology; D000918:Antibody Specificity; D005260:Female; D007031:Hypothalamus / Q000032:analysis*; D009842:Oligopeptides / Q000276:immunology*; D010446:Peptide Fragments / Q000032:analysis* / Q000276:immunology; D011498:Protein Precursors / Q000032:analysis*; D011863:Radioimmunoassay; D051381:Rats; D011919:Rats, Inbred Strains; D013973:Thyrotropin-Releasing Hormone / Q000032:analysis* / Q000276:immunology
D000906:Antibodies; D009842:Oligopeptides; D010446:Peptide Fragments; D011498:Protein Precursors; D013973:Thyrotropin-Releasing Hormone