Equine antibodies to Bothrops asper myotoxin II: isolation from polyvalent antivenom and neutralizing ability.

 

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Detalles Bibliográficos
Autores: Lomonte, Bruno, Gutiérrez, José María, Carmona Morera, Elena, Rovira Rodríguez, María Elena
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