![](/images/graphics-bg.png)
Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity from Bothrops barnetti Snake Venom
Joint Authors
Huancahuire-Vega, Salomón
Brousett-Minaya, Magaly Alejandra
Marangoni, Sérgio
Baldasso, Paulo Aparecido
Source
Issue
Vol. 2013, Issue 2013 (31 Dec. 2013), pp.1-11, 11 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2013-07-31
Country of Publication
Egypt
No. of Pages
11
Main Subjects
Pharmacy, Health & Medical Sciences
Biology
Medicine
Abstract EN
A thrombin-like enzyme named TLBbar was isolated from Bothrops barnetti snake venom and its biochemical and pharmacological characteristics were determined.
TLBbar was purified using size exclusion chromatography and reverse phase HPLC, showing molecular mass of 28750.7 Da determined by mass spectrometry.
TLBbar serine protease is basic (pI 7.4) and its structure shows similarity with other serine proteases of snake venom.
Optimal proteolytic activity was at 37°C and pH 8; this activity was strongly inhibited by PMSF and Leupeptin, however; heparin, and soybean trypsin inhibitor (SBT-I) were ineffective.
Kinetic studies on BApNA chromogenic substrate have revealed that TLBbar presents a Michaelis-Menten kinetics, with values of Km and Vmax of 0.433 mM and 0.42 nmol/min, respectively.
TLBbar showed high clotting activity upon bovine and human plasma, presenting IC of 125 and minimum dose coagulant (MDC) of 2.23 μg/μL.
TLBbar cleavages the Aα chain of bovine fibrinogen, with maximal efficiency at 30–40°C in the presence of calcium after two hours incubation; this fibronogenolityc activity was inhibited by PMSF and Leupeptin, confirming its classification in the group of serine proteases.
In addition, TLBbar is capable of aggregating platelets in the same way that thrombin in concentrations of 2.5 μg/μL.
American Psychological Association (APA)
Brousett-Minaya, Magaly Alejandra& Baldasso, Paulo Aparecido& Huancahuire-Vega, Salomón& Marangoni, Sérgio. 2013. Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity from Bothrops barnetti Snake Venom. Journal of Toxins،Vol. 2013, no. 2013, pp.1-11.
https://search.emarefa.net/detail/BIM-454525
Modern Language Association (MLA)
Brousett-Minaya, Magaly Alejandra…[et al.]. Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity from Bothrops barnetti Snake Venom. Journal of Toxins No. 2013 (2013), pp.1-11.
https://search.emarefa.net/detail/BIM-454525
American Medical Association (AMA)
Brousett-Minaya, Magaly Alejandra& Baldasso, Paulo Aparecido& Huancahuire-Vega, Salomón& Marangoni, Sérgio. Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity from Bothrops barnetti Snake Venom. Journal of Toxins. 2013. Vol. 2013, no. 2013, pp.1-11.
https://search.emarefa.net/detail/BIM-454525
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-454525