Isolation and characterization of a bradykinin-potentiating peptide from a bovine peptic hemoglobin hydrolysate.
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 alpha-chain of bovine hemoglobin. The bradykinin potency of this peptide, as exhibited by the guinea-pig ileum contraction, was significant and comparable with some others previously described.
Piot
J M
JM
Laboratoire de Technologie des Substances Naturelles, BP 179-IUT A Lille I, Villeneuve d'Ascq, France.
Zhao
Q
Q
Guillochon
D
D
Ricart
G
G
Thomas
D
D
D000595:Amino Acid Sequence; D000818:Animals; D001920:Bradykinin / Q000494:pharmacology*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D006168:Guinea Pigs; D006454:Hemoglobins / Q000737:chemistry* / Q000494:pharmacology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology; D016339:Spectrometry, Mass, Fast Atom Bombardment
D006454:Hemoglobins; D010446:Peptide Fragments; D001920:Bradykinin