Ser(13)-phosphorylated PYY from porcine intestine with a potent biological activity

We have isolated a posttranslationally modified form of peptide YY (PYY) from porcine intestine and shown by MALDI-TOF and electrospray tandem mass spectrometry that it is phosphorylated at Ser(13). Phospho-PYY exhibits high affinity for binding to neuropeptide Y (NPY) receptors Y1, Y2 and Y5. The I...

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Veröffentlicht in:	FEBS letters 2001-03, Vol.492 (1-2), p.119-122
Hauptverfasser:	Chen, Z, Eriste, E, Jonsson, A P, Norberg, A, Nepomuceno, D, Lovenberg, T W, Bergman, T, Efendic, S, Jörnvall, H, Sillard, R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Cyclic AMP - metabolism Humans Intestinal Mucosa - metabolism Peptide YY - chemistry Peptide YY - metabolism Phosphorylation Sequence Analysis, Protein Sequence Homology, Amino Acid Serine - metabolism Swine Tumor Cells, Cultured
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