Purification and characterization of galanin from the phylogenetically ancient fish, the bowfin (Amia calva) and dogfish (Scyliorhinus canicula)

Yunxia Wang, J. Michael Conlon

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Galanin was purified to near homogeneity from an extract of the stomachs of the holostean fish, the bowfin and the elasmobranch fish, the European common dogfish. Bowfin galanin contains an α-amidated C-terminal residue and the primary structure of the peptide (GWTNL SAGYL LGPHA VDNHR SLNDK HGLA) shows only four amino acid substitutions (Val16 → Ile, Leu22 → Phe, Asn23 → His, and His26 → Tyr) compared with pig galanin. Dogfish galanin was isolated in a truncated form for which amino acid sequence was identical to residues (1-20) of bowfin galanin. The isolation of this fragment is indicative of processing at the site of a single arginyl residue, and an analogous peptide has been previously isolated from human intestine. The data demonstrate that peptides with close structural similarity to mammalian galanins are present in the gastrointestinal tracts of phylogenetically ancient fish.

Original languageEnglish (US)
Pages (from-to)981-986
Number of pages6
JournalPeptides
Volume15
Issue number6
DOIs
StatePublished - 1994

Fingerprint

Dogfish
Galanin
Fish
Purification
Fishes
Peptides
Elasmobranchii
Amino Acids
Amino Acid Substitution
Intestines
Gastrointestinal Tract
Amino Acid Sequence
Stomach
Substitution reactions
Swine
Processing

Keywords

  • Amiiformes
  • Elasmobranch
  • Galanin
  • Stomach

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

Cite this

Purification and characterization of galanin from the phylogenetically ancient fish, the bowfin (Amia calva) and dogfish (Scyliorhinus canicula). / Wang, Yunxia; Conlon, J. Michael.

In: Peptides, Vol. 15, No. 6, 1994, p. 981-986.

Research output: Contribution to journalArticle

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N2 - Galanin was purified to near homogeneity from an extract of the stomachs of the holostean fish, the bowfin and the elasmobranch fish, the European common dogfish. Bowfin galanin contains an α-amidated C-terminal residue and the primary structure of the peptide (GWTNL SAGYL LGPHA VDNHR SLNDK HGLA) shows only four amino acid substitutions (Val16 → Ile, Leu22 → Phe, Asn23 → His, and His26 → Tyr) compared with pig galanin. Dogfish galanin was isolated in a truncated form for which amino acid sequence was identical to residues (1-20) of bowfin galanin. The isolation of this fragment is indicative of processing at the site of a single arginyl residue, and an analogous peptide has been previously isolated from human intestine. The data demonstrate that peptides with close structural similarity to mammalian galanins are present in the gastrointestinal tracts of phylogenetically ancient fish.

AB - Galanin was purified to near homogeneity from an extract of the stomachs of the holostean fish, the bowfin and the elasmobranch fish, the European common dogfish. Bowfin galanin contains an α-amidated C-terminal residue and the primary structure of the peptide (GWTNL SAGYL LGPHA VDNHR SLNDK HGLA) shows only four amino acid substitutions (Val16 → Ile, Leu22 → Phe, Asn23 → His, and His26 → Tyr) compared with pig galanin. Dogfish galanin was isolated in a truncated form for which amino acid sequence was identical to residues (1-20) of bowfin galanin. The isolation of this fragment is indicative of processing at the site of a single arginyl residue, and an analogous peptide has been previously isolated from human intestine. The data demonstrate that peptides with close structural similarity to mammalian galanins are present in the gastrointestinal tracts of phylogenetically ancient fish.

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