Resumen de Purification and Some Properties of Hemagglutinating Protein Mutina from Bushmaster Lachesis muta Snake Venom
M. A. Gómez Leiva, F. Aragón Ortiz
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.
