Fujita H, Usui H, Kurahashi K, Yoshikawa M
Nippon Synthetic Chemical Industry Co., Ltd., Osaka, Japan.
Peptides. 1995;16(5):785-90. doi: 10.1016/0196-9781(95)00054-n.
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.
经过三步反相高效液相色谱法，从卵清蛋白的胃蛋白酶消化物中纯化出一种血管舒张肽。该肽的结构为苯丙氨酸-精氨酸-丙氨酸-天冬氨酸-组氨酸-脯氨酸-苯丙氨酸-亮氨酸，对应于卵清蛋白的358-365位残基。该肽被命名为卵激肽。卵激肽对犬肠系膜动脉显示出舒张活性（半数有效浓度=6.3微摩尔）。缓激肽B1拮抗剂[去-精氨酸9][亮氨酸8]缓激肽可阻断其舒张活性，但B2拮抗剂Hoe 140则不能。卵激肽与B1受体结合（半数抑制浓度=64微摩尔）。卵激肽刺激后，动脉中作为舒张因子释放出前列腺素I2。因此，卵激肽是一种源自食物蛋白的弱缓激肽B1激动剂肽。
