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

Author 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
Institution FAPESP
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Abstract 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.
Keywords Lonomia obliqua
prothrombin activator
Language English
Date 2001-06-01
Published in Thrombosis Research. Oxford: Pergamon-Elsevier B.V., v. 102, n. 5, p. 427-436, 2001.
ISSN 0049-3848 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 427-436
Origin http://dx.doi.org/10.1016/S0049-3848(01)00265-1
Access rights Closed access
Type Article
Web of Science ID WOS:000169278900006
URI http://repositorio.unifesp.br/handle/11600/26569

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