Purification and substrate specificity of an angiotensin converting elastase-2 from the rat mesenteric arterial bed perfusate.

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.creatorPaula, Carmem Aparecida de-
Autor(es): dc.creatorSousa, Marcelo Valle de-
Autor(es): dc.creatorSalgado, Maria Cristina de Oliveira-
Autor(es): dc.creatorOliveira, Eduardo Brandt de-
Data de aceite: dc.date.accessioned2025-08-21T15:26:41Z-
Data de disponibilização: dc.date.available2025-08-21T15:26:41Z-
Data de envio: dc.date.issued2017-02-23-
Data de envio: dc.date.issued2017-02-23-
Data de envio: dc.date.issued1998-
Fonte completa do material: dc.identifierhttp://www.repositorio.ufop.br/handle/123456789/7306-
Fonte completa do material: dc.identifierhttp://www.sciencedirect.com/science/article/pii/S0167483898001861-
Fonte completa do material: dc.identifierhttps://doi.org/10.1016/S0167-4838(98)00186-1-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1014957-
Descrição: dc.descriptionA soluble angiotensin (Ang) II-generating enzyme has been purified to homogeneity from the rat mesenteric arterial bed(MAB) perfusate by a combination of gel filtration and affinity chromatographies. The enzyme is a glycoprotein of 28.5 kDa(SDS-PAGE), whose N-terminal sequence is identical with that of the rat pancreatic elastase-2 ; therefore the enzyme willhenceforth be referred to as rat MAB elastase-2. When Ang I was used as the substrate, the enzyme specifically released AngII and the dipeptide His-Leu (Km=36WM;Kcat= 1530 min31). The catalytic efficiency (Kcat/Km= 42.5 min31WM31) of thisreaction was comparable to those of other known Ang I-converting enzymes. The proteolytic specificity of the purifiedenzyme toward mellitin, oxidized insulin B chain, somatostatin-14 and renin substrate tetradecapeptide suggested that theenzyme-substrate interaction was defined by an extended substrate binding site, typical of elastases-2 of pancreatic origin. According to the sensitivity of the rat MAB elastase-2 to various inhibitors this enzyme could be described as a member ofthe chymostatin-sensitive group of Ang II-forming serine proteases. The localization and biochemical properties of thisenzyme suggest that it might play a role in the regional control of vascular tonus.-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Direitos: dc.rightsaberto-
Palavras-chave: dc.subjectChymase-
Palavras-chave: dc.subjectSomatostatin-
Título: dc.titlePurification and substrate specificity of an angiotensin converting elastase-2 from the rat mesenteric arterial bed perfusate.-
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