Biochemical and functional characterization of BmooSP, a new serine protease from Bothrops moojeni snake venom.

Autor: de Oliveira F; Instituto de Ciências Biomédicas, Universidade Federal de Uberlândia, Uberlândia MG, Brazil; Instituto Nacional de Ciência e Tecnologia em Nano-Biofarmacêutica (N-Biofar), Belo Horizonte MG, Brazil. Electronic address: foliveira@umuarama.ufu.br., de Sousa BB; Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, Uberlândia MG, Brazil; Instituto Nacional de Ciência e Tecnologia em Nano-Biofarmacêutica (N-Biofar), Belo Horizonte MG, Brazil., Mamede CC; Instituto de Ciências Biomédicas, Universidade Federal de Uberlândia, Uberlândia MG, Brazil; Instituto Nacional de Ciência e Tecnologia em Nano-Biofarmacêutica (N-Biofar), Belo Horizonte MG, Brazil., de Morais NC; Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, Uberlândia MG, Brazil; Instituto Nacional de Ciência e Tecnologia em Nano-Biofarmacêutica (N-Biofar), Belo Horizonte MG, Brazil., de Queiroz MR; Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, Uberlândia MG, Brazil; Instituto Nacional de Ciência e Tecnologia em Nano-Biofarmacêutica (N-Biofar), Belo Horizonte MG, Brazil., da Cunha Pereira DF; Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, Uberlândia MG, Brazil., Matias MS; Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, Uberlândia MG, Brazil., Homi Brandeburgo MI; Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, Uberlândia MG, Brazil.
Jazyk: angličtina
Zdroj: Toxicon : official journal of the International Society on Toxinology [Toxicon] 2016 Mar 01; Vol. 111, pp. 130-8. Date of Electronic Publication: 2016 Jan 13.
DOI: 10.1016/j.toxicon.2016.01.055
Abstrakt: In this work, we describe the purification and characterization of a new serine protease enzyme from Bothrops moojeni snake venom (BmooSP). On SDS-PAGE, BmooSP was found to be a single-chain protein with an apparent molecular mass of 36,000 and 32,000 under reduced and non-reduced conditions, respectively. Mass spectrometry analysis showed that the BmooSP is composed by two isoforms with molecular mass of 30,363 and 30,070, respectively. The purified enzyme consists of 277 amino acid residues, disregarding the cysteine and tryptophan residues that have been degraded by acid hydrolysis, and its N-terminal sequence showed similarity with other serine protease enzymes. BmooSP induced blood-clotting in vitro, defibrination in vivo, caseinolytic and fibrin(ogen)olytic activities. The enzyme is stable at high temperatures (up to 100 °C) and shows maximum activity at pH around 7.0. Preliminary results show that BmooSP can induce the formation of a stable fibrin clot for more than 10 days. BmooSP presents medical interest because it can be used as biodegradable fibrin glue and for the treatment and prevention of cardiovascular disorders because of its ability to promote the defibrination in vivo, decreasing blood viscosity and improving blood circulation.
(Copyright © 2016 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: