Characterization of Bothrops jararaca coagulation inhibitor (BjI) and presence of similar protein in plasma of other animals

Characterization of Bothrops jararaca coagulation inhibitor (BjI) and presence of similar protein in plasma of other animals

Author Tanaka-Azevedo, A. M. Google Scholar
Torquato, RJS Google Scholar
Tanaka, A. S. Google Scholar
Sano-Martins, I. S. Google Scholar
Institution Inst Butantan
Universidade Federal de São Paulo (UNIFESP)
Abstract BjI, a protein isolated from Bothrops jararaca snake blood, inhibits the coagulant activity of thrombin. This protein presents two bands of 109 and 138 kDa by SDS-PAGE under reducing conditions. in order to verify the presence of BjI-like proteins in plasma of other animals (reptiles and non-reptiles), we raised a specific polyclonal antibody in mice to it, and we verified immunological cross-reaction by western blotting, considering as positive reactions the development of bands with either 109 or 138 kDa. Similar proteins were identified in Bothrops neuwiedi and Crotalus durissus terrificus snakes. in contrast, no BjI-like protein in other classes of animals was noticeable, nor in other snakes tested. Interestingly, a prolonged thrombin time was found only in snake plasmas that showed similar BjI proteins. BjI bound to two proteins of B. jararaca venom, identified by western blotting. the N-terminal of the B. jararaca venom proteins showed similarity with thrombin-like proteins isolated from other snake venoms. in conclusion, there are similar proteins to BjI in plasmas of B. neuwiedi and Crotalus durissus terrificus, and these proteins also prolong thrombin time. Moreover, these results evidence the presence of target enzymes in snake venom for plasma BjI. (C) 2004 Elsevier B.V. All rights reserved.
Keywords blood coagulation
snake plasma
Bothrops jararaca
thrombin inhibitor
Language English
Date 2004-09-01
Published in Toxicon. Oxford: Pergamon-Elsevier B.V., v. 44, n. 3, p. 289-294, 2004.
ISSN 0041-0101 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 289-294
Origin http://dx.doi.org/10.1016/j.toxicon.2004.06.001
Access rights Closed access
Type Article
Web of Science ID WOS:000223572600008
URI http://repositorio.unifesp.br/handle/11600/27923

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