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

• Autores: M. A. Gómez Leiva, F. Aragón Ortiz
• Localización: Revista de Biología Tropical, ISSN 0034-7744, Vol. 34, Nº. 1, 1986 (Ejemplar dedicado a: Volume 34 – Regular number 1 – June 1986)
• Idioma: inglés
• Títulos paralelos:
  • Purification and Some Properties of Hemagglutinating Protein Mutina from Bushmaster Lachesis muta Snake Venom
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• Resumen

  • 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.