Characterization of the C-terminal flanking peptide of human β-preprotachykinin

Gerard P. McGregor, J. Michael Conlon

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3 Citations (Scopus)


The nucleotide sequence of cDNA encoding the common biosynthetic precursor of substance P, neurokinin A and neuropeptide K (β-preprotachykinin) predicts that, in the human, the precursor contains a C-terminal flanking peptide of 19 amino acid residues [β-preprotachykinin(111-129)-peptide]. Using an antiserum raised against synthetic human β-preprotachykinin(117-126)-peptide in radioimmunoassay, we have demonstrated that an extract of a human neuroendocrine tumor of the adrenal medulla contained approximately equimolar concentrations of C-terminal preprotachykinin immunoreactivity (C-PPT-IR), substance P and neurokinin A. The C-terminal preprotachykinin flanking peptide was purified to homogeneity and its primary structure was determined. The amino acid sequence of the peptide, Ala-Leu-Asn-Ser-Val-Ala-Tyr-Glu-Arg-Ser-Ala-Met-Gln-Asn-Tyr-Glu, indicates identity with β-preprotachykinin(111-126)-peptide. The data suggest that the C-terminal flanking peptide, like the tachykinins, is packed into secretory storage vesicles but the Arg127-Arg128-Arg129 residues in human β-preprotachykinin are removed from the peptide by the action of endogenous processing enzyme(s).

Original languageEnglish
Pages (from-to)907-910
Number of pages4
Issue number5
Publication statusPublished (in print/issue) - 1990


  • Neurokinin A
  • Pheochromocytoma
  • Preprotachykinin
  • Substance P


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