Boophilus microplus tick larvae, a rich source of Kunitz type serine proteinase inhibitors

Boophilus microplus tick larvae, a rich source of Kunitz type serine proteinase inhibitors

Author Sasaki, S. D. Google Scholar
Azzolini, SSA Google Scholar
Hirata, I. Y. Google Scholar
Andreotti, R. Google Scholar
Tanaka, A. S. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)
Abstract Serine 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.
Keywords serine proteinase inhibitors
Boophilus microplus
Language English
Date 2004-09-01
Published in Biochimie. Paris: Editions Scientifiques Medicales Elsevier, v. 86, n. 9-10, p. 643-649, 2004.
ISSN 0300-9084 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 643-649
Access rights Closed access
Type Article
Web of Science ID WOS:000225621600007

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