title: Purification and some properties of hemagglutinating protein mutina from bushmaster Lachesis muta snake venom.
abstract: Lachesis muta snake venom induced aggregation of bromelain sensitized human erythrocytes at 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 maximum peak (mutina) at 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. Lactose and inositol inhibited the agglutination of A, B, 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.
authors: Depto. de Bioquímica, Universidad de Costa Rica.
authors: M A
authors: MA
authors: Gómez Leiva
authors: F
authors: F
authors: Aragón-Ortiz
mesh_terms: D000371:Agglutination; D000818:Animals; D005591:Chemical Fractionation; D003435:Crotalid Venoms / Q000032:analysis*; D004912:Erythrocytes / Q000276:immunology; D006386:Hemagglutination Tests; D037102:Lectins / Q000302:isolation & purification*; D010974:Platelet Aggregation
chemical_list: D003435:Crotalid Venoms; D037102:Lectins