Characterization of an amidated form of pancreatic polypeptide from the daddy sculpin (Cottus scorpius)

J. M. Conlon, W. E. Schmidt, B. Gallwitz, S. Falkmer, L. Thim

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39 Citations (Scopus)

Abstract

The primary structure of pancreatic polypeptide from the teleostean fish, Cottus scorpius (daddy sculpin) was established as: Y P P Q P E S P G G N A S P E D W A K Y H A A V R H Y V N L I T R Q R Y NH2. The presence of a COOH-terminally α-amidated amino acid was established using an HPLC method of general applicability. Although the peptide shows strong homology towards anglerfish pancreatic polypeptide (86%), homology towards porcine peptide YY (PYY) (61%) and porcine neuropeptide Y (NPY) (61%) was greater than towards porcine pancreatic polypeptide (PP) (47%). This result supports suggestions that the gene duplication events which led to PP, NPY and PYY formation took place after the time of divergence of fish and mammals.

Original languageEnglish
Pages (from-to)261-268
Number of pages8
JournalRegulatory Peptides
Volume16
Issue number3-4
DOIs
Publication statusPublished (in print/issue) - 30 Dec 1986

Keywords

  • HPLC
  • primary structure
  • teleost pancreatic islet

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