Resumen

CAHUANA, Gladys; VIVAS, Dan; RODRIGUEZ, Edith  y  YARLEQUE, Armando. Purification and characteristics of bilineatobin, a clotting enzyme isolated from the venom of the arboreal peruvian snake Bothrops bilineatus (loro machaco). Rev. Soc. Quím. Perú [online]. 2012, vol.78, n.1, pp.43-52. ISSN 1810-634X.

A clotting enzyme was purified from Bothrops bilineatus arboreal snake venom, called bilineatobin, using Sephadex G-100 followed by CM Sephadex C-50, in both two cases with 0,05 M amonium acetate buffer pH 6,0. The enzyme was purified 24,8 fold with 16% of yield. The molecular weight obtained by molecular exclusion chromatographic was 40 kDa while by SDS-PAGE was 45 kDa. It is a monomeric protein with at least one disulfide bond and because its coagulant activity on fibrinogen, citrated human plasma as well as chromogenic substrate BApNA would be a trombin like enzyme. The amidolytic activity was stable until 60⁰C and optimum pH was 7,0. In addition the enzyme is inhibited by PMSF suggesting that is a serine proteinase and its inhibition by heparin indicates greater functional similarity to the protein thrombin counterparts in other ophidian poisons.

Palabras clave : Coagulant enzyme; venom; snake; Bothrops bilineatus; bilineatobin.

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