Isolation and characterization of ovokinin, a bradykinin B1 agonist peptide derived from ovalbumin

A vasorelaxing peptide was purified from a peptic digest of ovalbumin, after three steps of reverse-phase HPLC. The structure of the peptide was Phe-Arg-Ala-Asp-His-Pro-Phe-Leu, which corresponded to residues 358-365 of ovalbumin. The peptide was named ovokinin. Ovokinin showed relaxing activity for...

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Veröffentlicht in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 1995, Vol.16 (5), p.785-790
Hauptverfasser: Fujita, H, Usui, H, Kurahashi, K, Yoshikawa, M
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Sprache:eng
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Zusammenfassung:A vasorelaxing peptide was purified from a peptic digest of ovalbumin, after three steps of reverse-phase HPLC. The structure of the peptide was Phe-Arg-Ala-Asp-His-Pro-Phe-Leu, which corresponded to residues 358-365 of ovalbumin. The peptide was named ovokinin. Ovokinin showed relaxing activity for a canine mesenteric artery (EC50 = 6.3 microM). The relaxing activity was blocked by the bradykinin B1 antagonist [des-Arg9] [Leu8]bradykinin, but not by the B2 antagonist Hoe 140. Ovokinin binds to B1 receptors (IC50 = 64 microM). Prostaglandin I2 was released from the artery after ovokinin stimulation as a relaxing factor. Thus, ovokinin is a weak bradykinin B1 agonist peptide derived from food proteins.
ISSN:0196-9781
DOI:10.1016/0196-9781(95)00054-n