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

Toxicon : Official Journal of the International Society on Toxinology
Fábio de OliveiraMaria Inês Homi Brandeburgo

Abstract

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 improvin...Continue Reading

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Citations

Nov 9, 2016·Toxicon : Official Journal of the International Society on Toxinology·Yang YuePengcheng Li
Nov 26, 2019·Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis·Amel Kadi-Saci, Fatima Laraba-Djebari
Mar 8, 2017·Proceedings of the National Academy of Sciences of the United States of America·Chuchu ZhangDavid Julius
Apr 30, 2021·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Déborah Fernanda da Cunha PereiraCarla Cristine Neves Mamede

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