Carassin: A Tachykinin That Is Structurally Related to Neuropeptide‐γ from the Brain of the Goldfish

J. Michael Conlon, Finbarr O'Harte, Richard E. Peter, Olivier Kah

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)

Abstract

Abstract: A 21‐amino‐acid residue tachykinin‐related peptide, carassin, was isolated in pure form from an extract of the brain of the goldfish, Carrassius auratus, by reversedphase HPLC. The primary structure of the peptide was established as the following: Ser‐Pro‐Ala‐Asn‐Ala‐Gln‐IIe‐Thr‐Arg ‐ Lys ‐ Arg ‐ His ‐ Lys ‐ Hle ‐ Asn ‐ Ser ‐ Phe ‐ Val ‐ Gly ‐ Leu‐Met · NH2. This amino acid sequence is the same length as and shows structural similarity (57% homology) to the mammalian tachykinin, neuropeptide‐γ, which is a product of the posttranslational processing of γ‐preprotachykinin. The mammalian tachykinins, substance P and neurokinin B, were not detected in the extract by using specific antisera directed against the NH2‐termini of the peptides, but an antiserum directed against the COOH‐terminal region of substance P did detect a low concentration of immunoreactive material.

Original languageEnglish
Pages (from-to)1432-1436
Number of pages5
JournalJournal of Neurochemistry
Volume56
Issue number4
DOIs
Publication statusPublished - Apr 1991

Keywords

  • Goldfish brain
  • Neuropeptideγ
  • Scyliorhinin II
  • Tachykinin

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