High molecular weight kininogen as substrate for cathepsin B

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dc.contributor.author Barros, NMT
dc.contributor.author Tersariol, ILS
dc.contributor.author Oliva, MLV
dc.contributor.author Araujo, M. S.
dc.contributor.author Sampaio, CAM
dc.contributor.author Juliano, L.
dc.contributor.author Motta, G. da
dc.date.accessioned 2016-01-24T12:37:12Z
dc.date.available 2016-01-24T12:37:12Z
dc.date.issued 2004-06-01
dc.identifier http://dx.doi.org/10.1515/BC.2004.066
dc.identifier.citation Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 385, n. 6, p. 551-555, 2004.
dc.identifier.issn 1431-6730
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/27791
dc.description.abstract We investigated the influence of pH and divalent cations (Zn2+, Mg2+ and Ca2+) on high molecular weight kininogen processing by cathepsin B. At pH 6.3, high molecular weight kininogen is hydrolyzed by cathepsin B at three sites generating fragments of 80, 60 and 40 kDa. Cathepsin B has kininogenase activity at this pH which is improved in the absence of divalent cations. At pH 7.35, high molecular weight kininogen is slightly cleaved by cathepsin B into fragments of 60 kDa, and cathepsin B kininogenase activity is impaired. Our results suggest that high molecular weight kininogen is a substrate for cathepsin B under pathophysiological conditions. en
dc.format.extent 551-555
dc.language.iso eng
dc.publisher Walter de Gruyter & Co
dc.relation.ispartof Biological Chemistry
dc.rights Acesso restrito
dc.subject cystatins en
dc.subject cysteine peptidase en
dc.subject kinin en
dc.subject zinc en
dc.title High molecular weight kininogen as substrate for cathepsin B en
dc.type Artigo
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution UMC
dc.description.affiliation UNIFESP, EPM, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliation UMC, Ctr Interdisciplinar Invest Bioquim, BR-08701970 Mogi Das Cruzes, SP, Brazil
dc.description.affiliation UNIFESP, EPM, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifesp UNIFESP, EPM, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifesp UNIFESP, EPM, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.identifier.doi 10.1515/BC.2004.066
dc.description.source Web of Science
dc.identifier.wos WOS:000222500200015



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