Purification and some properties of hemagglutinating protein mutina from bushmaster Lachesis muta snake venom.
Rev Biol Trop
; 34(1): 49-53, 1986 Jun.
Article
em En
| MEDLINE
| ID: mdl-3671807
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Venenos de Crotalídeos
/
Lectinas
Limite:
Animals
Idioma:
En
Revista:
Rev Biol Trop
Ano de publicação:
1986
Tipo de documento:
Article
País de publicação:
Costa Rica