ISOLATION AND PARTIAL CHARACTERIZATION OF TWO PROTEASES FROM THE VENOM OF PERUVIAN Loxosceles laeta SPIDER

• Autores: Huari, Frank, Lazo, Fanny, Vivas, Dan, Rodríguez, Edith, Yarlequé, Armando
• Formato: artículo
• Fecha de Publicación: 2016
• Institución: Sociedad Química del Perú
• Repositorio: Revista de la Sociedad Química del Perú
• Lenguaje: español
• OAI Identifier: oai:rsqp.revistas.sqperu.org.pe:article/60
• Enlace del recurso: http://revistas.sqperu.org.pe/index.php/revistasqperu/article/view/60
• Nivel de acceso: acceso abierto
• Materia: Venom; spider; proteases; procoagulant; antivenom; Veneno; araña; proteasa; procoagulante; antiveneno

Two proteases from the glandular venom of Loxosceles laeta spider were isolated using a column of Sephadex G-100 gel molecular filtration equilibrated with 0,05M ammonium acetate buffer pH 5,0. One of them is a metalloprotease inhibited by 5 mM EDTA (60,5%) and the other is a serinoprotease inhibited by 5 mM PMSF (93,3%). The metalloproteinase had activity on casein and dimethylcasein while the serinoprotease had activity on citrated human plasma. They showed different molecular weights by PAGE-SDS: 35 kDa and 15,9 kDa. In addition both were antigenic against commercial loxoscelic antivenom by immunodifusion assays.