| Literature DB >> 2897223 |
D Graff1, C J Grimmelikhuijzen.
Abstract
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.Entities:
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Year: 1988 PMID: 2897223 DOI: 10.1016/0006-8993(88)91525-9
Source DB: PubMed Journal: Brain Res ISSN: 0006-8993 Impact factor: 3.252