Isolation and characterization of a bradykinin‐potentiating peptide from a bovine peptic hemoglobin hydrolysate

FEBS Letters

Guillochon, Didier³  Zhao, Qiuyu³  Piot, Jean-Marie³  Ricart, Guy¹  Thomas, Daniel² 

[1] Laboratoire de Spectrométrie de Masse, Lille I, 59655 Villeneuve d'Ascq Cédex, France;Laboratoire de Technologie Enzymatique, URA 1442 du CNRS, Université de Technologie de Compiègne, BP 649, Compiègne Cédex, France;Laboratoire de Technologie des Substances Naturelles, BP 179 — IUT A Lille I, 59653 Villeneuve d'Ascq Cédex, France

关键词: Bovine hemoglobin;    Bradykinin potentiation;    Peptic hydrolysate;    High-performance liquid chromatography;    Mass spectrometry;   

DOI  :  10.1016/0014-5793(92)80104-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A bradykinin potentiating peptide was isolated from a peptic bovine hemoglobin hydrolysate, by the use of reversed-phase high-performance liquid chromatography (RP-HPLC). Its primary structure, determined by fast atom bombardment (FAB) and tandem mass spectrometry (MS/MS), was identical to fragment 129–134 of the α-chain of bovine hemoglobin. The bradykinin potency of this peptide, as exhibited by the guinea-pis ileum contraction, was significant and comparable with some others previously described.

【 授权许可】

Unknown