A C-terminally elongated form of PHI from porcine intestine

E. Eriste, Å Norberg, V. Bonetto, D. Nepomuceno, T. W. Lovenberg, R. Sillard, H. Jörnvall

Research output: Contribution to journalArticlepeer-review


A C-terminally elongated form of peptide histidine isoleucine amide (PHI) was isolated from porcine intestine based on its effect on cAMP production in IMR-32 cells. The structure was determined by amino acid sequence analysis of tryptic fragments and by mass spectrometry. The peptide has 42 amino acid residues like those described from human, rat and mouse, but the amino acid sequence of the C-terminal extension of pig PHI is unique. Unlike the other peptides, it has a C-terminal Ala and it differs at five positions from the human form and at six positions from the rat form, while the human and the rat forms differ by only two substitutions. To avoid confusion arising from different C-terminal residues, a unifying nomenclature is proposed: PHI-27 for the hormone and PHI-42 for the elongated product.

Original languageEnglish
Pages (from-to)709-713
Number of pages5
JournalCellular and Molecular Life Sciences
Issue number7-8
Publication statusPublished - 1999


  • cAMP production
  • Prohormone processing
  • VIP/PHI precursor

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Cell Biology


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