The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity
Research output: Contribution to journal › Journal article › Research › peer-review
Neuropeptides containing the C-terminal sequence Arg-Phe-NH2 (RFamide) occur throughout the Animal Kingdom and are abundant in evolutionarily 'old' nervous systems such as those of cnidarians. From the hydromedusa Polyorchis penicillatus we have previously isolated two neuropeptides, Pol-RFamide I (
| Original language | English |
|---|---|
| Journal | Biochemical Journal |
| Volume | 299 ( Pt 2) |
| Issue number | 299 |
| Pages (from-to) | 431-436 |
| Number of pages | 6 |
| ISSN | 0264-6021 |
| Publication status | Published - 15 Apr 1994 |
- Amino Acid Sequence, Animals, Base Sequence, Biological Evolution, Cnidaria, Endopeptidases, Gene Library, Insect Hormones, Molecular Sequence Data, Neuropeptides, Oligodeoxyribonucleotides, Protein Precursors, Protein Processing, Post-Translational, Protein Sorting Signals, Restriction Mapping, Sequence Homology, Amino Acid
Research areas
ID: 248899