SciELO - Scientific Electronic Library Online

vol.83 issue4Optimization of medium composition for extracelluar proteases production by Pseudomonas sp. in submerged fermentarion author indexsubject indexarticles search
Home Pagealphabetic serial listing  

Services on Demand




  • Have no cited articlesCited by SciELO

Related links

  • Have no similar articlesSimilars in SciELO


Revista de la Sociedad Química del Perú

Print version ISSN 1810-634X


RUIZ, Luis et al. Purification, Biochemical and Biological Characterization of the Thrombin-Like Enzyme Present in the Venom of the Snake Bothrops brazili. Rev. Soc. Quím. Perú [online]. 2017, vol.83, n.4, pp.463-474. ISSN 1810-634X.

A coagulant enzyme from Bothrops brazili snake venom called thrombin-like enzyme was purified by three successive chromatographic steps on Sephadex G-75, DEAE Sephadex A-50 and Sephadex G-50 using 0.05M Tris-HCl buffer pH 8.5. The enzyme was purified 15.9 times with a yield of 28.6% and by PAGE-SDS a single protein band of 48 kDa was obtained both in reducing and non-reducing conditions using 2β-Mercaptoethano., It is a unicatenary protein with coagulant activity on both citrated human plasma and bovine fibrinogen. The enzyme showed amidolytic activity on the chromogenic substrate Benzoyl-Arginyl-p- Nitroaniline (BApNA) and the coagulant potency on bovine fibrinogen was calculated on 121 NIH units of thrombin / mg. The enzyme was inhibited by PMSF and the soybean trypsin inhibitor, therefore, it is a serine protease; the optimum pH for the amidolytic activity was 8.5 and the protein was stable to heat treatment only up to 40 °C. The minimal defibrinogenating dose was 8 μg / g of mouse and by double immunodiffusion tests immunoreactivity was observed with respect to INS polyvalent antibothropic serum

Keywords : Bothrops brazili; Thrombin-like enzyme; snake; venom; coagulation.

        · abstract in Spanish     · text in Spanish     · Spanish ( pdf )


Creative Commons License All the contents of this journal, except where otherwise noted, is licensed under a Creative Commons Attribution License