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.
Originalsprog | Engelsk |
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Tidsskrift | Brain Research |
Vol/bind | 442 |
Udgave nummer | 2 |
Sider (fra-til) | 354-8 |
Antal sider | 5 |
ISSN | 0006-8993 |
Status | Udgivet - 1 mar. 1988 |