Open AccessIsolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon--secretin family.
Author(s) -
Kazuhiko Tatemoto,
Viktor Mutt
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.11.6603
Subject(s) - secretin , secretin family , vasoactive intestinal peptide , peptide , peptide sequence , biochemistry , amino acid , chemistry , peptide hormone , glucagon , gastrointestinal hormone , biology , hormone , neuropeptide , secretion , receptor , gene
A new peptide, designated PHI (PHI-27), has been discovered and isolated from porcine upper intestinal tissue by using a chemical method for finding peptide hormones and other active peptides. The method is based on chemical detection of peptides having the cOOH-terminal alpha-amide structure, which is an unusual chemical feature of some peptide hormones and active peptides. Porcine PHI was found in the intestinal extract by the presence of its COOH-terminal isoleucine amide structure. It consists of 27 amino acid residues and has the following amino acid sequence: His-Ala-Asp-Gly-Val-Phe-Thr-Ser-Asp-Phe-Ser-Arg-Leu-Leu-Gly-Gln-Leu-Ser-Ala-Lys -Lys-Tyr-Leu-Glu-Ser-Leu-Ile-NH2. The remarkable sequence homology of PHI to the vasoactive intestinal peptide, secretin, glucagon, and gastric inhibitory polypeptide indicates that this peptide is a member of the glucagon-secretin family. Several biological activities of PHI, similar to those of vasoactive intestinal peptide and secretin, have been reported.