A double headed serine proteinase inhibitor - human plasma kallikrein and elastase inhibitor - from Boophilus microplus larvae

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dc.contributor.authorTanaka, A. S.
dc.contributor.authorAndreotti, R.
dc.contributor.authorGomes, A.
dc.contributor.authorTorquato, RJS
dc.contributor.authorSampaio, M. U.
dc.contributor.authorSampaio, CAM
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionEmpresa Brasileira de Pesquisa Agropecuária (EMBRAPA)
dc.date.accessioned2016-01-24T12:30:57Z
dc.date.available2016-01-24T12:30:57Z
dc.date.issued1999-12-01
dc.description.abstractPreying on cattle, the hard tick Boophilus microplus causes heavy economical losses to Brazil. Tick proteins are a good target to be used as tools for tick control. Serine protease inhibitors from B. microplus larvae (BmTI) were preliminarily characterized. One-week-old larvae were the source of a 2% protein solution in 5 mM Tris-HCl, 20 mM NaCl, pH 7.4. the inhibitors were purified by affinity chromatography on trypsin-Sepharose, and ion-exchange chromatography on Resource Q column, and they separated in two major active peaks, corresponding to 10-kDa and 18-kDa proteins (BmTI-B and BmTI-A, respectively). Both purified proteins inhibited trypsin with K-i of 0.3 and 3.0 nM, respectively, but only the 18-kDa protein inhibited elastase (K-i 1.4 nM) and plasma kallikrein (K-i 120 nM). BmTI-A did not change prothrombin time (PT) and thrombin time (TT), but it increased activated partial thromboplastin time (APTT) was dose-dependent. the partial amino acid sequence indicated that BmTI-A belongs to the bovine pancreatic trypsin inhibitor (BPTI)-Kunitz type inhibitor family. These inhibitors (by their properties) play a role in the feeding process of the tick. Development of antibodies against these proteins may be used to impair the normal feeding and consequently, the parasite would be no longer viable. (C) 1999 Elsevier Science B.V. All rights reserved.en
dc.description.affiliationUNIFESP, EPM, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationEMBRAPA, CNPGC, C Grande, MS, Brazil
dc.description.affiliationUnifespUNIFESP, EPM, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent171-177
dc.identifierhttp://dx.doi.org/10.1016/S0162-3109(99)00074-0
dc.identifier.citationImmunopharmacology. Amsterdam: Elsevier B.V., v. 45, n. 1-3, p. 171-177, 1999.
dc.identifier.doi10.1016/S0162-3109(99)00074-0
dc.identifier.issn0162-3109
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26186
dc.identifier.wosWOS:000084080100028
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofImmunopharmacology
dc.rightsAcesso restrito
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectserine proteinase inhibitorsen
dc.subjectticken
dc.subjectblood coagulationen
dc.subjectAPTTen
dc.titleA double headed serine proteinase inhibitor - human plasma kallikrein and elastase inhibitor - from Boophilus microplus larvaeen
dc.typeArtigo
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