Questions, Feedback & Help
Send us an email and we'll get back to you ASAP. Or you can read our Frequently Asked Questions.
  • page settings
  • hide sidebar
  • show empty fields
  • layout
  • (too narrow)
  • open all
  • close all
Resources » Paper

Marks NJ et al. (1995) Biochem Biophys Res Commun "Isolation of AF2 (KHEYLRFamide) from Caenorhabditis elegans: evidence for the presence of more than one FMRFamide-related peptide-encoding gene."

  • History

  • Referenced

  • Tree Display

  • My Favorites

  • My Library

  • Comments on Marks NJ et al. (1995) Biochem Biophys Res Commun "Isolation of AF2 (KHEYLRFamide) from Caenorhabditis elegans: evidence for the presence of more than one FMRFamide-related peptide-encoding gene." (0)

  • Overview

    PMID:
    Status:
    Publication type:
    Journal_article
    WormBase ID:
    WBPaper00002356

    Marks NJ, Shaw C, Maule AG, Davis JP, Halton DW, Verhaert P, Geary TG, & Thompson DP (1995). Isolation of AF2 (KHEYLRFamide) from Caenorhabditis elegans: evidence for the presence of more than one FMRFamide-related peptide-encoding gene. Biochem Biophys Res Commun, 217, 845-51. doi:10.1006/bbrc.1995.2849

    Numerous FMRF amide-related peptides (FaRPs) have been isolated and sequenced from extracts of free-living and parasitic nematodes. The most abundant FaRP identified in ethanolic/methanolic extracts of the parasitic forms, Ascaris suum and Haemonchus contortus and from the free-living nematode, Panagrellus redivivus, was KHEYLRF amide (AF2). Analysis of the nucleotide sequences of cloned FaRP-precursor genes from C. elegans and, more recently, Caenorhabditis vulgaris identified a series of related FaRPs which did not include AF2. An acid-ethanol extract of Caenorhabditis elegans was screened radioimmunometrically for the presence of FaRPs using a C-terminally directed FaRP antiserum. Approximately 300 pmols of the most abundant immunoreactive peptide was purified to homogeneity and 30 pmols was subjected to Edman degradation analysis and gas-phase sequencing. The unequivocal primary structure of the heptapeptide, Lys-His-Glu-Tyr-Leu-Arg-Phe-NH2 (AF2) was determined following a single gas-phase sequencing run. The molecular mass of the peptide was determined using a time-of-flight mass spectrometer and was found to be 920 (MH(+))(-), which was consistent with the theoretical mass of C-terminally amidated AF2. These results indicate that C. elegans possesses more than one FaRP gene.

    Authors: Marks NJ, Shaw C, Maule AG, Davis JP, Halton DW, Verhaert P, Geary TG, Thompson DP

    Affiliation:
    - Comparative Neuroendocrinology Research Group, Queen's University of Belfast, Northern Ireland.

    Keywords:
    Tip: Seeing your name marked red? Please help us identify you.