Some biochemical and biological properties of C- Type Lectin from Peruvian Lachesis muta snake venom

Abstract

Some properties of a C-type lectin purified from the venom of L. muta was carried out. In this way the venom was fractionated into Sephadex G-100 gel filtration chromatography using 0.05 M ammonium acetate buffer pH 5. The effect of temperatura 30-60 °C and pH in the range of 4 to 9 were assayed through hemagglutination activity. In addition antigenic action was preformed lachesic antivenom by double immunodiffusion. Besides toxicity as well as blood coagulation effect on human plasma were determinated. As results of this investigation, this lectin was purified 12,7 folds after 0,1 M lactose applied with 5,4% of recovering active protein. This lectin is very stable because of change of temperatura and pH no modified its original activity. In addition C-type lectin show antigenic reaction against lachesic antivenom but has not toxic action due to inyection into peritoneal via on mice (50 to 200 µg) not produce neither mortality nor tissue damages. Finally assays with this protein on human citrated plasma, no affect its recalcification time. Therefore C-type lectin from L. muta venom could participate on the envenomation scheme due a strong association with red cells in a wide range of pH and temperature.