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.
Original language | English |
---|---|
Journal | Brain Research |
Volume | 442 |
Issue number | 2 |
Pages (from-to) | 354-8 |
Number of pages | 5 |
ISSN | 0006-8993 |
Publication status | Published - 1 Mar 1988 |
Keywords
- Animals
- Chromatography, High Pressure Liquid
- Cnidaria
- Neurons
- Neuropeptides
- Oligopeptides
- Pyrrolidonecarboxylic Acid
- Sea Anemones