Purification and Some Properties of Hemagglutinating Protein Mutina from Bushmaster Lachesis muta Snake Venom
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| Autores: | , |
|---|---|
| Formato: | artículo original |
| Estado: | Versión publicada |
| Fecha de Publicación: | 1986 |
| Descripción: | 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. |
| País: | Portal de Revistas UCR |
| Institución: | Universidad de Costa Rica |
| Repositorio: | Portal de Revistas UCR |
| Lenguaje: | Inglés |
| OAI Identifier: | oai:portal.ucr.ac.cr:article/24355 |
| Acceso en línea: | https://revistas.ucr.ac.cr/index.php/rbt/article/view/24355 |