Immobilized analogues of sunflower trypsin inhibitor-1 constitute a versatile group of affinity sorbents for selective isolation of serine proteases (2009)
- Autores:
- Autores USP: SALGADO, MARIA CRISTINA DE OLIVEIRA - FMRP ; OLIVEIRA, EDUARDO BRANDT DE - FMRP
- Unidade: FMRP
- DOI: 10.1016/j.jchromb.2009.05.036
- Assunto: BIOQUÍMICA
- Idioma: Inglês
- Imprenta:
- Fonte:
- Título do periódico: Journal of Chromatography B
- ISSN: 1570-0232
- Volume/Número/Paginação/Ano: v. 877, n. 22, p. 2039-2044, 2009
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
ABNT
PEREIRA, Hugo Juarez Vieira e SALGADO, Maria Cristina de Oliveira e OLIVEIRA, Eduardo Brandt de. Immobilized analogues of sunflower trypsin inhibitor-1 constitute a versatile group of affinity sorbents for selective isolation of serine proteases. Journal of Chromatography B, v. 877, n. 22, p. 2039-2044, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.jchromb.2009.05.036. Acesso em: 19 set. 2024. -
APA
Pereira, H. J. V., Salgado, M. C. de O., & Oliveira, E. B. de. (2009). Immobilized analogues of sunflower trypsin inhibitor-1 constitute a versatile group of affinity sorbents for selective isolation of serine proteases. Journal of Chromatography B, 877( 22), 2039-2044. doi:10.1016/j.jchromb.2009.05.036 -
NLM
Pereira HJV, Salgado MC de O, Oliveira EB de. Immobilized analogues of sunflower trypsin inhibitor-1 constitute a versatile group of affinity sorbents for selective isolation of serine proteases [Internet]. Journal of Chromatography B. 2009 ; 877( 22): 2039-2044.[citado 2024 set. 19 ] Available from: https://doi.org/10.1016/j.jchromb.2009.05.036 -
Vancouver
Pereira HJV, Salgado MC de O, Oliveira EB de. Immobilized analogues of sunflower trypsin inhibitor-1 constitute a versatile group of affinity sorbents for selective isolation of serine proteases [Internet]. Journal of Chromatography B. 2009 ; 877( 22): 2039-2044.[citado 2024 set. 19 ] Available from: https://doi.org/10.1016/j.jchromb.2009.05.036 - Angiotensin I metabolism: differences between the rat mesenteric bed and cardiac perfusates
- The early phase of pressure-overload cardiac hypertrophy is associated with an increased breakdown of bradykinin in the rat cardiac perfusate
- 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
- Angiotensin I metabolism in cardiac perfusate of aortic-banded rats
- 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
- Alternative pathways for angiotensin II generation in the cardiovascular system
Informações sobre o DOI: 10.1016/j.jchromb.2009.05.036 (Fonte: oaDOI API)
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