A prothrombin activator serine protease from the Lonomia obliqua caterpillar venom (Lopap) biochemical characterization

A prothrombin activator serine protease from the Lonomia obliqua caterpillar venom (Lopap) biochemical characterization

Autor Reis, C. V. Google Scholar
Portaro, FCV Google Scholar
Andrade, S. A. Google Scholar
Fritzen, M. Google Scholar
Fernandes, B. L. Google Scholar
Sampaio, CAM Google Scholar
Camargo, ACM Google Scholar
Chudzinski-Tavassi, A. M. Google Scholar
Instituição FAPESP
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Resumo Lonomia obliqua venom causes a severe consumptive coagulopathy, which can lead to a hemorrhagic syndrome. the crude bristles extract displays a procoagulant activity due to a Factor X and to a prothrombin activating activity. Here, we describe a 69 kDa prothrombin activator serine protease purified from L. obliqua caterpillar bristle extract using gel filtration (Sephadex G 75) and HPLC (C-4 column). the purified protein was able to activate prothrombin in a dose-dependent manner, and calcium ions increased this activity. the prothrombin-derived fluorogenic peptide (Abz-YQTFFNPRTGSQ-EDDnp) had its main cleavage site at the Arg-Thr bond. the kinetic parameters obtained for this substrate were K-mapp. of 4.5 muM, k(cat) of 5.32 s(-1), and a k(cat)/K-mapp of 1.2 x 10(6) M-1 s(-1). the prothrombin fragments generated by the purified enzyme corresponded to the molecular masses of prethrombin 2, fragment 1, fragment 2, and thrombin as seen in SDS-PAGE. the thrombin generated was able to clot purified fibrinogen. the partial amino acid sequence of the purified protein, named Lopap (L. obliqua prothrombin activator protease), showed no similarity to any known prothrombin activator. (C) 2001 Elsevier B.V. All rights reserved.
Assunto Lonomia obliqua
prothrombin activator
Idioma Inglês
Data 2001-06-01
Publicado em Thrombosis Research. Oxford: Pergamon-Elsevier B.V., v. 102, n. 5, p. 427-436, 2001.
ISSN 0049-3848 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 427-436
Fonte http://dx.doi.org/10.1016/S0049-3848(01)00265-1
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000169278900006
URI http://repositorio.unifesp.br/handle/11600/26569

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