A high molecular weight precursor of luteinizing hormone releasing hormone from rat hypothalamus

A poly A+ enriched fraction of total RNA extracted from rat hypothalamus was translated in a messenger RNA-dependent cell free system from rabbit reticulocyte lysate supplemented with 3H-leucine. The translation products were immunoprecipitated using a specific antiserum to luteinizing hormone releasing hormone (LHRH). Following sodium dodecyl sulphate polyacrylamide gel electrophoresis and autoradiography of the immunoprecipitates, a single immunoreactive polypeptide was detected with an apparent molecular weight of 28,000. This is approximately twenty times larger than the active peptide, and thus suggests the presence of a high molecular weight precursor for the decapeptide, LHRH.