Toxicon : official journal of the International Society on Toxinology · 2016
Expression and partial biochemical characterization of a recombinant serine protease from Bothrops pauloensis snake venom.
СтатьяПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод в очереди
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Isabel Thais F, Costa Guilherme Nunes Moreira, Pacheco Isabela B, Barbosa Luana G, Santos-Junior Célio D, Fonseca Fernando P P, Boldrini França Johara, Henrique-Silva Flávio, Yoneyama Kelly A G, Rodrigues Renata S, Rodrigues Veridiana de Melo
Аннотация
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.