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

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

Autor Tanaka, A. S. Google Scholar
Andreotti, R. Google Scholar
Gomes, A. Google Scholar
Torquato, RJS Google Scholar
Sampaio, M. U. Google Scholar
Sampaio, CAM Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)
Resumo Preying 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.
Palavra-chave serine proteinase inhibitors
blood coagulation
Idioma Inglês
Data de publicação 1999-12-01
Publicado em Immunopharmacology. Amsterdam: Elsevier B.V., v. 45, n. 1-3, p. 171-177, 1999.
ISSN 0162-3109 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 171-177
Fonte http://dx.doi.org/10.1016/S0162-3109(99)00074-0
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000084080100028
Endereço permanente http://repositorio.unifesp.br/handle/11600/26186

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