Angiotensin processing is partially carried out by carboxypeptidases in the rat mesenteric arterial bed perfusate (2008)
- Authors:
- USP affiliated authors: SALGADO, MARIA CRISTINA DE OLIVEIRA - FMRP ; OLIVEIRA, EDUARDO BRANDT DE - FMRP
- Unidade: FMRP
- DOI: 10.1016/j.regpep.2008.09.003
- Subjects: BIOQUÍMICA; ARTÉRIAS; SISTEMA RENINA-ANGIOTENSINA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Regulatory Peptides
- ISSN: 0167-0115
- Volume/Número/Paginação/Ano: v. 151, n. 1-3, p. 135-138, 2008
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
ABNT
PEREIRA, Hugo J. V. et al. Angiotensin processing is partially carried out by carboxypeptidases in the rat mesenteric arterial bed perfusate. Regulatory Peptides, v. 151, n. 1-3, p. 135-138, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.regpep.2008.09.003. Acesso em: 20 maio 2024. -
APA
Pereira, H. J. V., Souza, L. L., Salgado, M. C. de O., & Oliveira, E. B. de. (2008). Angiotensin processing is partially carried out by carboxypeptidases in the rat mesenteric arterial bed perfusate. Regulatory Peptides, 151( 1-3), 135-138. doi:10.1016/j.regpep.2008.09.003 -
NLM
Pereira HJV, Souza LL, Salgado MC de O, Oliveira EB de. Angiotensin processing is partially carried out by carboxypeptidases in the rat mesenteric arterial bed perfusate [Internet]. Regulatory Peptides. 2008 ; 151( 1-3): 135-138.[citado 2024 maio 20 ] Available from: https://doi.org/10.1016/j.regpep.2008.09.003 -
Vancouver
Pereira HJV, Souza LL, Salgado MC de O, Oliveira EB de. Angiotensin processing is partially carried out by carboxypeptidases in the rat mesenteric arterial bed perfusate [Internet]. Regulatory Peptides. 2008 ; 151( 1-3): 135-138.[citado 2024 maio 20 ] Available from: https://doi.org/10.1016/j.regpep.2008.09.003 - Angiotensin I metabolism: differences between the rat mesenteric bed and cardiac perfusates
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- Angiotensin I metabolism in cardiac perfusate of aortic-banded rats
- Immobilized analogues of sunflower trypsin inhibitor-1 constitute a versatile group of affinity sorbents for selective isolation of serine proteases
- Functional role, cellular source, and tissue distribution of rat elastase-2, an angiotensin II-forming enzyme
- Potentiation of bradykinin effect by angiotensin-converting enzyme inhibition does not correlate with angiotensin-converting enzyme activity in the rat mesenteric arteries
- Isolation of angiotensin II-forming serine protease from the rat cardiac vascular bed perfusate
- Isolation of an angiotensin II-forming serine protease from the rat cardiac vascular bed perfusate
- Angiotensin-converting enzyme inhibition augments the expression of rat elastase-2, an angitensin II-forming enzyme
- Kinetic characterization and inhibition of the rat MAB elastase-2, an angiotensin I-converting serine protease
Informações sobre o DOI: 10.1016/j.regpep.2008.09.003 (Fonte: oaDOI API)
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