Isolation and primary structure of gastrin-releasing peptide from a teleost fish, the trout (Oncorhynchus mykiss)

Jorgen Jensen, J. Michael Conlon

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)


Immunohistochemical studies have established that fish gastrointestinal tissues contain peptides with gastrin-releasing peptide (GRP)/bombesin-like immunoreactivity, but the molecular nature of this material is unclear. In this study, the most abundant peptide that was immunoreactive towards an antiserum raised against pig GRP was isolated in pure form from an extract of the stomach of the rainbow trout (Oncorhynchus mykiss). The primary structure of the peptide was established as: Ser-Glu-Asn-Thr-Gly-Ala-Ile-Gly-Lys-Val10-Phe-Pro-Arg-Gly-Asn-His-Trp-Ala-Val-Gly20-His-Leu-Met-NH2. Although this amino acid sequence is shorter than those of mammalian GRPs by four residues, the COOH-terminal dodecapeptide is identical to the corresponding region in pig GRP. The data indicate, therefore, that the predominant molecular form of GRP in the stomach of a teleost fish is structurally more similar to mammalian GRP than to the amphibian skin peptide, bombesin.

Original languageEnglish
Pages (from-to)995-999
Number of pages5
Issue number5
Publication statusPublished - 1992
Externally publishedYes


  • Bombesin
  • Evolution
  • Gastrin-releasing peptide
  • Stomach
  • Trout

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience


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