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A novel bradykinin potentiating peptide isolated from Bothrops jararacussu venom using catallytically inactive oligopeptidase EP24.15
Author(s) -
Rioli Vanessa,
Prezoto Benedito C.,
Konno Katsuhiro,
Melo Robson L.,
Klitzke Clécio F.,
Ferro Emer S.,
FerreiraLopes Mônica,
Camargo Antonio C. M.,
Portaro Fernanda C. V.
Publication year - 2008
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2008.06389.x
Subject(s) - bradykinin , peptide , venom , chemistry , snake venom , oligopeptidase , bothrops , biochemistry , pharmacology , enzyme , biology , receptor
Characterization of the peptide content of venoms has a number of potential benefits for basic research, clinical diagnosis, development of new therapeutic agents, and production of antiserum. Here, we use a substrate‐capture assay that employs a catalytically inactive mutant of thimet oligopeptidase (EC 3.4.24.15; EP24.15) to identify novel bioactive peptides in Bothrops jararacussu venom. Of the peptides captured with inactive EP24.15 and identified by mass spectrometry, three were previously identified bradykinin‐potentiating peptides (BPP),