Scyliorhinin I and II: two novel tachykinins from dogfish gut

J. Michael Conlon, Carolyn F. Deacon, Liam O'Toole, Lars Thim

Research output: Contribution to journalArticlepeer-review

103 Citations (Scopus)

Abstract

Two peptides with tachykinin-like ability to contract longitudinal muscle from the guinea pig ileum were isolated from the intestine of the common dogfish, Scyliorhinus caniculus. The amino acid sequence of scyliorhinin I was established as Ala-Lys-Phe-Asp-Lys-Phe-Tyr-Gly-Leu-Met-NH2 and this peptide cross-reacted with antisera directed against the C-terminal region fo substance P. The amino acid sequence of scyliorhinin II was established as Ser-Pro-Ser-Asn-Ser-Lys-Cys-Pro-Asp-Gly-Pro-Asp-Cys-Phe-val-Gly-Leu-Met-NH2 and this peptide cross-reacted with antisera directed against the C-terminal region of neurokinin A. The mammalian peptides substance P and neurokinin A were absent from the dogfish intestinal tissue.

Original languageEnglish
Pages (from-to)111-116
Number of pages6
JournalFEBS Letters
Volume200
Issue number1
DOIs
Publication statusPublished - May 5 1986
Externally publishedYes

Keywords

  • Scyliorhinin (Dogfish) Substance P Neurokinin A Tachykinin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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