Abstract

HUARI, Frank et al. Isolation and partial characterization of two proteases from the venom of peruvian Loxosceles laeta spider. Rev. Soc. Quím. Perú [online]. 2016, vol.82, n.3, pp.296-305. ISSN 1810-634X.

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.

Keywords : Venom; spider; proteases; procoagulant; antivenom.

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