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Physalaemin-like immunoreactive peptides from rabbit stomach.

W E Wilson, D J Harvan, C Hamm

    International Journal of Peptide and Protein Research
    |July 1, 1986
    PubMed
    Summary
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    Researchers purified two physalaemin (PHY)-like peptides (PHLIPs) from rabbit stomachs. Their sequences were determined, revealing homology with amphibian PHY, suggesting a conserved function.

    Area of Science:

    • Biochemistry
    • Peptide Chemistry
    • Mammalian Physiology

    Background:

    • Physalaemin (PHY) is a bioactive peptide found in amphibian skin.
    • The existence and function of PHY-like peptides in mammals have not been fully elucidated.
    • Rabbit stomach tissue is a potential source for novel peptide discovery.

    Purpose of the Study:

    • To identify and characterize physalaemin (PHY)-like immunoreactive peptides in rabbit stomach extracts.
    • To determine the amino acid sequences of these novel peptides.
    • To investigate the structural homology and potential cross-reactivity with physalaemin antiserum.

    Main Methods:

    • Peptide purification from rabbit stomach tissue extracts.
    • Fast atom bombardment/mass spectrometry (FAB/MS) for molecular weight determination.

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  • FAB/tandem MS, amino acid analysis, and computational methods for sequence elucidation.
  • Confirmation of peptide sequences using synthetic peptide standards.

    • Main Results:

    • Two physalaemin (PHY)-like immunoreactive peptides, designated PHLIPs, were successfully purified.
    • Mass spectrometry identified protonated molecular ions at m/z 867.419 and 796.4.
    • Amino acid sequencing revealed the primary structures of PHLIPs-7 and PHLIPs-8.
    • PHLIPs exhibited cross-reactivity with PHY-antiserum, indicating homology at key residues (1, 3, 4, 5).

    Conclusions:

    • Novel mammalian physalaemin (PHY)-like peptides (PHLIPs) have been identified in rabbit stomach.
    • The determined sequences confirm the presence of PHY-homologous peptides in mammals.
    • Observed cross-reactivity suggests conserved functional roles or structural motifs between amphibian and mammalian PHY-like peptides.