Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2007855 | Peptides | 2006 | 10 Pages |
Abstract
Hemorphins are biologically active peptides, derived from hemoglobin, which presents a number of physiological activities. Proteolytic generation of these peptides is not fully understood; however, among their roles, is to provoke reduction on blood pressure. In this work, this particular biological effect was chosen as the monitor for the selection of mammalian vasoactive peptides. By combining high-performance liquid chromatography and mass spectrometry, including 'de novo' sequencing, several hemorphin-like peptides were identified presenting bradykinin potentiating activity. Moreover, taking LVV-hemorphin-7 as model compound, we evaluated its biological effect on blood pressure of anaesthetized rats. By summarizing all the results, it is possible to present the hemorphins as a family of proteolytically generated peptides that are able to potentiate bradykinin activity in vivo.
Keywords
TFABradykinin potentiating peptideBothrops jararacaACEACNODSMALDI-TOFAngiotensin IAngiotensin-I Converting EnzymeAngiotensin IIAcetonitrileTrifluoroacetic acidEndopeptidasebradykininde novo sequencingAng IIMass spectrometrymatrix-assisted laser desorption ionization time of flightAng IHemorphinHemoglobinHPLChigh-performance liquid chromatography
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Danielle Ianzer, Katsuhiro Konno, Carlos Henrique Xavier, Reto Stöcklin, Robson Augusto S. Santos, Antônio Carlos Martins de Camargo, Daniel Carvalho Pimenta,