KSAYMRFamide (PF3/AF8) is present in the free-living nematode, Caenorhabditis elegans

Nicola Marks, Aaron Maule, T.G. Geary, D.P. Thompson, C. Li, David Halton, Christopher Shaw

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

To date, seven FMRFamide-related peptides (FaRPs) have been structurally characterized from C. elegans, of which one is structurally identical to the parasitic nematode peptide AF2 (KHEYLRFamide). The other six FaRPs have so far been identified in free-living forms only. in the present study an additional FaRP was isolated and structurally characterized from an ethanolic extract of C. elegans. The extract was screened using a C-terminally directed FaRP antiserum, and the FMRFamide-immunoreactive peptide purified to homogeneity using HPLC. Approximately 80 pmol of the peptide was subjected to Edman degradation and the unequivocal primary structure of the K-7-amide, KSAYMRFamide (PF3/AF8) was determined following a single gas-phase sequencing run. The molecular mass of the peptide was determined using a MALDI-TOF mass spectrometer and was found to be 919 (MH+), which is in agreement with the theoretical mass of C-terminally amidated PF3. A new flp-gene, designated flp-6, has recently been identified which encodes six copies of KSAYMRFamide (PF3/AF8). (C) 1998 Academic Press.
Original languageEnglish
Pages (from-to)422-425
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume248
Issue number2
Publication statusPublished - 20 Jul 1998

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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