Isolation of less than Glu-Ser-Leu-Arg-Trp-NH2, a novel neuropeptide from sea anemones

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Using a radioimmunoassay for the peptide sequence Arg-Phe-NH2, a peptide has been purified from acetic acid extracts of the sea anemone Anthopleura elegantissima. This peptide has the structure less than Glu-Ser-Leu-Arg-Trp-NH2. Using antisera to its carboxyterminal sequence Arg-Trp-NH2, the peptide was found to be exclusively localized in neurons of sea anemones, among them neurons associated with the sphincter muscle. This suggest that the peptide is a transmitter at neuromuscular junctions.
Original languageEnglish
JournalBrain Research
Issue number2
Pages (from-to)354-8
Number of pages5
Publication statusPublished - 1 Mar 1988

    Research areas

  • Animals, Chromatography, High Pressure Liquid, Cnidaria, Neurons, Neuropeptides, Oligopeptides, Pyrrolidonecarboxylic Acid, Sea Anemones

ID: 33514506