Purification and Some Properties of Hemagglutinating Protein Mutina from Bushmaster Lachesis muta Snake Venom

Lachesis muta snake venom induced aggregation of bromelain sensitized human erythrocytes al a concentration of 1 mg/ml. The hemagglutinating protein was purified by DEAE-Sephadex A-50 column chromatography. Polyacrylamide gel electrophoresis revealed at least three bands, whereas SDS electrophoresis in the presence of 2-mercaptoethanol showed a single one. Isoelectric focusing revealed hemagglutinating activity in the range of pH 3-8. The maximun peak (mutina) al pH 5.5. This fraction was active in agglutinating human RBC of types A, B. O Rh (+) and B. O Rh (-).One mM EDTA and 1 mM Ca++ did not alter the agglutinating time significantly. Lactase and inositol inhibited the agglutination of A, S, O Rh (+) and B, O Rh (-) human RBC. The present study showed the non specificity of the hemagglutinating activity of mutina. It was also shown that mutina is a non-mitogenic protein.