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Isolation and characterization of a bradykinin‐potentiating peptide from a bovine peptic hemoglobin hydrolysate
Author(s) -
Piot Jean-Marie,
Zhao Qiuyu,
Guillochon Didier,
Ricart Guy,
Thomas Daniel
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80104-o
Subject(s) - hydrolysate , chemistry , bradykinin , hemoglobin , peptide , chromatography , fast atom bombardment , biochemistry , mass spectrometry , hydrolysis , receptor
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.

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