Abstract
We have isolated and sequenced the neuropeptide L-3-phenyllactyl-Phe-Lys-Ala-NH2 from the sea anemone Anthopleura elegantissima. This neuropeptide (named Antho-KAamide) has the unusual N-terminal L-3-phenyllactyl blocking group which has recently also been discovered in 2 other neuropeptides from sea anemones. We propose that the L-3-phenyllactyl residue renders Antho-KAamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the neuropeptide after neuronal release. The existence of the L-3-phenyllactyl residue in 3 neuropeptides isolated so far suggests that this blocking group is more generally occurring.
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Biochemical and Biophysical Research Communications |
| Vol/bind | 179 |
| Udgave nummer | 3 |
| Sider (fra-til) | 1205-11 |
| Antal sider | 7 |
| ISSN | 0006-291X |
| Status | Udgivet - 30 sep. 1991 |