Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity from <i>Bothrops barnetti</i> Snake Venom

<table>Chromatographic profile of the purification procedure and purity assay of TLBbar. (a) Molecular exclusion chromatography on Sephadex G-75. (110 × 4.0 cm) from <i>B. barnetti </i>snake venom. Fraction Bbt Ia (–) showed coagulant and proteolityc activities upon bovine fibrinogen and BApNA substrate, respectively. (b) Elution profile of Bbt Ia fraction by RP-HPLC on an analytical Supelco C8 column. Fraction 11 (TLBbar) showed high serine protease enzymatic activity with properties thrombin-like. Insert: electrophoretic profile in SDS-PAGE: (MM) molecular mass markers, (11-nr) TLBbar not reduced, (11-r) TLBbar reduced with DTT (1 M). (c) Rechromatography on RP-HPLC of TLBbar.</table>

Journal of Toxins

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Figure 1

Figure 1: Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity from <i>Bothrops barnetti</i> Snake Venom 

Figure 1 | Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity from Bothrops barnetti Snake Venom 