Isolation of less than Glu-Ser-Leu-Arg-Trp-NH2, a novel neuropeptide from sea anemones.
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.
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003063:Cnidaria; D009474:Neurons / Q000032:analysis; D009479:Neuropeptides / Q000302:isolation & purification*; D009842:Oligopeptides / Q000302:isolation & purification*; D011761:Pyrrolidonecarboxylic Acid / Q000031:analogs & derivatives; D012615:Sea Anemones
D009479:Neuropeptides; D009842:Oligopeptides; C056018:Antho-RWamide I; D011761:Pyrrolidonecarboxylic Acid