title: Characterization of an amidated form of pancreatic polypeptide from the daddy sculpin (Cottus scorpius).
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.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005399:Fishes / Q000378:metabolism*; D009478:Neuropeptide Y / Q000032:analysis; D010191:Pancreatic Polypeptide / Q000032:analysis* / Q000302:isolation & purification; D019894:Peptide YY; D010455:Peptides / Q000032:analysis
chemical_list: D000596:Amino Acids; D009478:Neuropeptide Y; D010455:Peptides; D019894:Peptide YY; D010191:Pancreatic Polypeptide