Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/27473
Title: Biochemical and pharmacological aspects of two bradykinin-potentiating peptides obtained from tryptic hydrolysis of casein
Authors: Perpetuo, Elen Aquino
Juliano, Luis [UNIFESP]
Lebrun, Ivo
Butantan Inst
Universidade Federal de São Paulo (UNIFESP)
Keywords: angiotensin-converting enzyme
bradykinin
casein
potentiating peptides
Issue Date: 1-Nov-2003
Publisher: Kluwer Academic/plenum Publ
Citation: Journal of Protein Chemistry. New York: Kluwer Academic/plenum Publ, v. 22, n. 7-8, p. 601-606, 2003.
Abstract: Peptides that display bradykinin-potentiating activity have been obtained from a number of distinct sources, such as snake venoms, fibrinogen, and casein. This paper describes the characterization of two new peptides generated by tryptic hydrolysis of casein. No homology was found with other known vasoactive or vasopotentiating peptides, especially by the lack of Ile-Pro-Pro motif. the peptides EMPFPK and YPVEPFTE, corresponding to the gamma casein sequence (108-113 and 114-121, respectively), displayed a selective potentiating activity on isolated guinea pig ileum for bradykinin. Besides, the octapeptide YPVEPFTE showed an in vitro competitive inhibitor effect on angiotensin-converting enzyme and thimet oligopeptidase and presented an opiate-like activity, increasing two times the latence time in the hot-plate assay. the results suggest that the isolated bioactive peptides act on conversion and/or inactivation of endogenous peptides by enzymes such as angiotensin-converting enzyme and thimet oligopeptidase by modifying several systemic responses such as blood-pressure regulation and in pain response.
URI: http://repositorio.unifesp.br/handle/11600/27473
ISSN: 0277-8033
Other Identifiers: http://dx.doi.org/10.1023/B:JOPC.0000008724.98339.ff
Appears in Collections:Artigo

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