SciELO - Scientific Electronic Library Online

vol.82 issue3Influence of lees presence during the resting time of base wine in some volatile compounds of peruvian Italia grape piscoDigestibility and digestible energy of five tropical forage tree legumes author indexsubject indexarticles search
Home Pagealphabetic serial listing  

Services on Demand




  • Have no cited articlesCited by SciELO

Related links

  • Have no similar articlesSimilars in SciELO


Revista de la Sociedad Química del Perú

Print version ISSN 1810-634X


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.

        · abstract in Spanish     · text in Spanish     · Spanish ( pdf )