Isolation of the tachykinin, Des[Ser1Pro2] scyliorhinin II from the intestine of the ray, Torpedo marmorata

J. Michael Conlon, Lars Thim

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19 Citations (Scopus)

Abstract

A peptide with neurokinin A-like immunoreactivity was isolated from an extract of the intestine of an elasmobranch fish, Torpedo marmorata. The primary structure of the peptide was established as Ser-Asn-Ser-Lys-Cys-Pro-Asp-Gly-Pro-Asp-Cys-Phe-Val-Gly-Leu-Met-NH2 . This amino acid sequence is identical to that of residues (3-18) of scyliorhinin II previously isolated from the intestine of the common dogfish (Scyliorhinus canicula). The presence of the truncated peptide, lacking Ser-Pro, in the Torpedo gut suggests that scyliorhinin II may be a substrate for an enzyme with dipeptidylpeptidase IV-like specificity. The data support previous assertions that strong evolutionary pressure has acted within the elasmobranch subclass of chondrichthyean fish to conserve the structures of regulatory peptides.

Original languageEnglish
Pages (from-to)383-388
Number of pages6
JournalGeneral and Comparative Endocrinology
Volume71
Issue number3
DOIs
Publication statusPublished - Sep 1988
Externally publishedYes

ASJC Scopus subject areas

  • Animal Science and Zoology
  • Endocrinology

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