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

Regul Pept. 1986 Dec 30;16(3-4):261-8. doi: 10.1016/0167-0115(86)90025-x.

Abstract

The primary structure of pancreatic polypeptide from the teleostean fish, Cottus scorpius (daddy sculpin) was established as: YPPQPESPGGNASPEDWAKYHAAVRHYVNLITRQRYNH2 The presence of a COOH-terminally alpha-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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Fishes / metabolism*
  • Neuropeptide Y / analysis
  • Pancreatic Polypeptide / analysis*
  • Pancreatic Polypeptide / isolation & purification
  • Peptide YY
  • Peptides / analysis

Substances

  • Amino Acids
  • Neuropeptide Y
  • Peptides
  • Peptide YY
  • Pancreatic Polypeptide