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Structural characterization of canine PYY.

V E Eysselein·G A Eberlein·D Grandt·M Schaeffer·B Zehres·U Behn·D Schaefer·H Goebell·M Davis·T D Lee
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Abstract

PYY was purified from canine colonic mucosa by sequential steps of reverse phase HPLC and ion-exchange FPLC. Microsequence, amino acid and mass spectral analyses of the purified peptide and its tryptic fragments were consistent with the structure: YPAKPEAPGEDASPEELSRYYASLRHYLNLVTRQRY-amide. Canine PYY(1-36) has the identical sequence as porcine and rat PYY but differs from human PYY at position 3, with Ala instead of Ile, and position 18, with Ser instead of Asn. A smaller form, PYY(3-36), was also purified and characterized. It may differ in its biological activity from the intact peptide and could act as a partial antagonist or agonist of PYY(1-36).

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Amino Acid SequenceAmino AcidsAnimalsChromatography, High Pressure LiquidColonDogsGastrointestinal HormonesHumansMass SpectrometryMolecular Sequence DataPeptide FragmentsPeptide YYPeptidesRadioimmunoassayRatsSpecies SpecificitySwineTrypsinJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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V E Eysselein, G A Eberlein, D Grandt, M Schaeffer, B Zehres, U Behn, D Schaefer, H Goebell, M Davis, T D Lee. Structural characterization of canine PYY.. https://doi.org/10.1016/0196-9781(90)90118-o

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