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dc.contributor.authorSasaki, S. D.
dc.contributor.authorAzzolini, SSA
dc.contributor.authorHirata, I. Y.
dc.contributor.authorAndreotti, R.
dc.contributor.authorTanaka, A. S.
dc.date.accessioned2016-01-24T12:37:20Z
dc.date.available2016-01-24T12:37:20Z
dc.date.issued2004-09-01
dc.identifierhttp://dx.doi.org/10.1016/j.biochi.2004.09.010
dc.identifier.citationBiochimie. Paris: Editions Scientifiques Medicales Elsevier, v. 86, n. 9-10, p. 643-649, 2004.
dc.identifier.issn0300-9084
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/27910
dc.description.abstractSerine proteinase inhibitors from Boophilus microplus tick larvae (BmTIs) were purified by affinity chromatography on a trypsin-Sepharose column. BmTIs presented molecular weight between M, 6200 and 18,400 and inhibitory activity for trypsin, HuPK (human plasma kallikrein) and neutrophil elastase. Using ion exchange chromatography, BmTIs were separated in several protein pools named BmTI-A to BmTI-F and BmTI-1 to BmTI-7. All BmTI forms presented inhibitory activity for trypsin with apparent dissociation constants (K-i) in the nM range. in this work, we describe the purification of BmTI-D, BmTI-2, and BmTI-3. These three inhibitors affected neutrophil elastase and HuPK with K-i also in nM range. BMTI-D proved to be the best HuPK inhibitor, while BmTI-3 was more efficient for neutrophil elastase with dissociation constants (K-i) of 12 and 0.5 nM, respectively. BmTI-D. BmTI-2, and BmTI-3 N-terminal amino acid sequences allowed us to include them into the BPTI-Kunitz type serine proteinase inhibitor family. BmTIs purified on trypsin-Sepharose were also used in a bovine immunization assay, resulting in antibody (anti-BmTIs) production. (C) 2004 Elsevier SAS. All rights reserved.en
dc.format.extent643-649
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimie
dc.rightsAcesso restrito
dc.subjectserine proteinase inhibitorsen
dc.subjectticken
dc.subjectectoparasiteen
dc.subjectBoophilus microplusen
dc.titleBoophilus microplus tick larvae, a rich source of Kunitz type serine proteinase inhibitorsen
dc.typeArtigo
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionEmpresa Brasileira de Pesquisa Agropecuária (EMBRAPA)
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, Escola Paulista Med, BR-04044020 São Paulo, Brazil
dc.description.affiliationEMBRAPA, CNPGC, Campo Grande, MS, Brazil
dc.description.affiliationUNIFESP, EPM, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, Escola Paulista Med, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUNIFESP, EPM, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.identifier.doi10.1016/j.biochi.2004.09.010
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000225621600007


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