SciELO - Scientific Electronic Library Online

vol.78 issue1Chromium (VI) adsorption with activated carbons prepared from wood chips of eucaliytus by chemical activation 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


RODRIGUEZ, Edith; SANDOVAL, Gustavo A.  and  YARLEQUE, Armando. Isolation and biochemical characterization of bilinearin, a prothrombin-activator factor from Bothrops bilineatus (loro machaco) peruvian snake venom. Rev. Soc. Quím. Perú [online]. 2012, vol.78, n.1, pp.3-13. ISSN 1810-634X.

A prothrombin activator, called bilinearin, has been detected and isolated from Bothrops bilineatus (loro machaco) snake venom. For its isolation, a combination of two chromatographical steps, CM Sephadex C-50 followed by Sephadex G-100 SF in ammonium acetate buffer 05 M pH 7,0. This enzyme was purified 10,4 times with a yield of 78,3%, and a recovery of 7,5%. Furthermore, it was determined that its molecular weight is 23-kDa, and is formed by 2 polypeptide chains, and 8,4% of attached carbohydrates. Bilinearin is a procoagulant enzyme capable of attacking commercial prothrombin in a direct manner without addition of Ca2+ or phospholipids, producing an active thrombin with clotting activity on human plasma. It was also determined that bilinearin is a metalloprotease because of its strong inhibition by EDTA and EGTA. This enzyme was also inhibited by 2-mercaptoetanol and after exposition to 55ºC, although it was only active until 45ºC. Finally, bilinearin is an immunogenic protein as demonstrated by its reaction to polyvalent bothropic antivenom (INS-Peru) using immunodiffusion and immunoelectrophoresis.

Keywords : Bothrops bilineatus; venom; prothrombin; clotting.

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