A novel bradykinin potentiating peptide isolated from Bothrops jararacussu venom using catallytically inactive oligopeptidase EP24.15.
FEBS J
; 275(10): 2442-54, 2008 May.
Article
en En
| MEDLINE
| ID: mdl-18400032
ABSTRACT
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),
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Endopeptidasas
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Péptidos
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Bradiquinina
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Inhibidores de la Enzima Convertidora de Angiotensina
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Bothrops
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Venenos de Crotálidos
Límite:
Animals
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Humans
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Male
Idioma:
En
Año:
2008
Tipo del documento:
Article