Resumo

RODRIGUEZ, Edith; SANDOVAL, Gustavo A.  e  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.

Palavras-chave : Bothrops bilineatus; venom; prothrombin; clotting.

        · resumo em Espanhol     · texto em Espanhol     · Espanhol ( pdf )