Equine antibodies to Bothrops asper myotoxin II: isolation from polyvalent antivenom and neutralizing ability.
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Autores: | , , , |
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Formato: | artículo original |
Fecha de Publicación: | 1990 |
Descripción: | Equine antibodies to B. riper myotoxin II were isolated from polyvalent antivenom by affinity chromatography. Purified antibodies were among the most acidic serum immunoglobulins, migrating between the ß- and aZ-globulin regions by zone electrophoresis . This might be related to the fact that myotoxin II is a very basic antigen. At an antibody/toxin molar ratio of two or higher, myotoxic effect of myotoxin II was neutralized completely . Antibodies also neutralized myotoxic activity of crude venom in mice, reducing the effect by about 75% when a proportion of 16 mg antibodies/mg venom was tested . Despite the lack of phospholipase AZ activity of myotoxin II, antibodies were able to neutralize this enzymatic activity of myotoxin I, a previously described isoform. This finding is in agreement with the notion that myotoxin II is a phospholipase AZ-analog devoid of this enzyme activity. |
País: | Kérwá |
Institución: | Universidad de Costa Rica |
Repositorio: | Kérwá |
OAI Identifier: | oai:kerwa.ucr.ac.cr:10669/73008 |
Acceso en línea: | http://www.sciencedirect.com/science/article/pii/004101019090075I https://hdl.handle.net/10669/73008 |
Palabra clave: | Antivenom Antibodies Neutralizing abilities |