Isolation and characterization of a myotoxin from Bothrops brazili Hoge, 1953 Hoge, 1953 snake venom (Ophidia: Viperidae).

• Autores: Pantigoso, Carmen, Escobar, Enrique, Yarlequé, Armando
• Formato: artículo
• Fecha de Publicación: 2001
• Institución: Universidad Nacional Mayor de San Marcos
• Repositorio: Revista UNMSM - Revista Peruana de Biología
• Lenguaje: español
• OAI Identifier: oai:ojs.csi.unmsm:article/6716
• Enlace del recurso: https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/6716
• Nivel de acceso: acceso abierto
• Materia: myotoxin; Bothrops brazili; snake venom; myonecrosis.; miotoxina; veneno de serpiente; mionecrosis.

A myotoxin from the venom of the snake Bothrops brazili has been purified by ion-exchange chromatography on CM-Sephadex C-50 with 0,05 M ammonium acetate buffer pH 7. The homogeneity was evaluated by PAGE with and without SDS, immunodiffusion and immunoelectrophoresis. The myotoxin is a basic protein with 15,6% of Lys+Arg; it is not a glicoprotein, has not enzymatic activity, and corresponds to 25% of the whole venom protein. The molecular weight of the myotoxin was determined by PAGE-SDS and gel filtration chromatography. The myotoxin has 30 KDa of molecular weight and two polypeptide chains of 15 KDa each. Myotoxin produces a severe necrosis on the gastrocnemius muscle of white mice. The myotoxin does not have hemolytic nor anticoagulant activity. However, produces edema with a DEM of 32,6 mg of protein.