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Structural characterization of canine PYY.

V E Eysselein1, G A Eberlein, D Grandt

  • 1Harbor-UCLA Medical Center, Department of Gastroenterology, Torrance 90509.

Peptides
|January 1, 1990
PubMed
Summary
This summary is machine-generated.

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Researchers purified and characterized canine PYY (Peptide YY) from colonic mucosa. Canine PYY shares sequence identity with porcine and rat PYY but differs from human PYY, with a smaller form also identified.

Area of Science:

  • Biochemistry
  • Peptide Chemistry
  • Comparative Genomics

Background:

  • Peptide YY (PYY) is a gastrointestinal hormone involved in appetite regulation.
  • Understanding species-specific PYY structures is crucial for comparative physiology and drug development.

Purpose of the Study:

  • To purify and determine the primary structure of canine Peptide YY (PYY).
  • To compare the canine PYY sequence with homologous peptides from other species.
  • To identify and characterize potential truncated forms of canine PYY.

Main Methods:

  • Purification of PYY from canine colonic mucosa using reverse-phase HPLC and ion-exchange FPLC.
  • Structural elucidation via microsequencing, amino acid analysis, and mass spectrometry.
  • Tryptic digestion and fragment analysis for detailed structural confirmation.

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Main Results:

  • Canine PYY(1-36) was purified and its sequence determined as YPAKPEAPGEDASPEELSRYYASLRHYLNLVTRQRY-amide.
  • Canine PYY(1-36) sequence is identical to porcine and rat PYY.
  • Canine PYY differs from human PYY at positions 3 (Ala vs. Ile) and 18 (Ser vs. Asn).
  • A smaller form, canine PYY(3-36), was also purified and characterized.

Conclusions:

  • The primary structure of canine PYY(1-36) has been established.
  • Canine PYY exhibits significant sequence homology with other mammalian PYY orthologs.
  • The identified canine PYY(3-36) may possess distinct biological activities compared to the full-length peptide.