Biochemical and functional characterization of BmooSP, a new serine protease from Bothrops moojeni snake venom. (1st March 2016)
- Record Type:
- Journal Article
- Title:
- Biochemical and functional characterization of BmooSP, a new serine protease from Bothrops moojeni snake venom. (1st March 2016)
- Main Title:
- Biochemical and functional characterization of BmooSP, a new serine protease from Bothrops moojeni snake venom
- Authors:
- de Oliveira, Fábio
de Sousa, Bruna Barbosa
Mamede, Carla Cristine Neves
de Morais, Nadia Cristina Gomes
de Queiroz, Mayara Ribeiro
da Cunha Pereira, Déborah F.
Matias, Mariana S.
Homi Brandeburgo, Maria Inês - Abstract:
- 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 improving blood circulation. Highlights: We describe the purification/characterisation of a new serine protease from B. moojeni (BmooSP). This protease is able to form a stable fibrin clot (fibrin glue). BmooSP can be used as tool for the studyAbstract: 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. Highlights: We describe the purification/characterisation of a new serine protease from B. moojeni (BmooSP). This protease is able to form a stable fibrin clot (fibrin glue). BmooSP can be used as tool for the study about cardiovascular disorders. … (more)
- Is Part Of:
- Toxicon. Volume 111(2016)
- Journal:
- Toxicon
- Issue:
- Volume 111(2016)
- Issue Display:
- Volume 111, Issue 1 (2016)
- Year:
- 2016
- Volume:
- 111
- Issue:
- 1
- Issue Sort Value:
- 2016-0111-0001-0000
- Page Start:
- 130
- Page End:
- 138
- Publication Date:
- 2016-03-01
- Subjects:
- Snake venom -- Bothrops moojeni -- Serine protease
Toxins -- Periodicals
Venom -- Periodicals
615.9 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00410101 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.toxicon.2016.01.055 ↗
- Languages:
- English
- ISSNs:
- 0041-0101
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8873.050000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 663.xml