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BIBTEX RIS

Expression and partial biochemical characterization of a recombinant serine protease from Bothrops pauloensis snake venom

2016; Elsevier BV; Volume: 115; Linguagem: Inglês

10.1016/j.toxicon.2016.03.002

1879-3150

Thaís Ferreira Isabel, Guilherme Nunes Moreira Costa, Isabela B. Pacheco, Luana Gonçalves Barbosa, Célio Dias Santos Júnior, Fernando P.P. Fonseca, Johara Boldrini-França, Flávio Henrique‐Silva, Kelly Aparecida Geraldo Yoneyama, Renata Santos Rodrigues, Veridiana de Melo Rodrigues,

Biochemical and Structural Characterization

Snake venom serine proteases (SVSPs) are enzymes capable of interfering at several points of hemostasis. Some serine proteases present thrombin-like activity, which makes them targets for the development of therapeutics agents in the treatment of many hemostatic disorders. In this study, a recombinant thrombin-like serine protease, denominated rBpSP-II, was obtained from cDNA of the Bothrops pauloensis venom gland and was characterized enzymatically and biochemically. The enzyme rBpSP-II showed clotting activity on bovine plasma and proteolytic activity on fibrinogen, cleaving exclusively the Aα chain. The evaluation of rBpSP-II activity on chromogenic substrates demonstrated thrombin-like activity of the enzyme due to its capacity to hydrolyze the thrombin substrate. These characteristics make rBpSP-II an attractive molecule for additional studies. Further research is needed to verify whether rBpSP-II can serve as a template for the synthesis of therapeutic agents to treat hemostatic disorders.