Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10880311 | Toxicon | 2005 | 7 Pages |
Abstract
Caprylic acid purification of IgG, currently used in the manufacture of horse-derived antivenoms, was successfully adapted for the preparation of sheep and camel IgG. Sheep IgG had a molecular mass of â¼150Â kDa, whereas camel IgG presented two bands of molecular masses of â¼160 and 100Â kDa, the latter corresponding to heavy-chain IgG, which is devoid of light chains. Horse, sheep and camel IgGs were compared by several parameters aiming at predicting their potential for induction of early and late adverse reactions. Horse and sheep IgGs showed a higher anticomplementary activity than camel IgG, and also elicited a higher anti-IgG response than camel IgG, when injected in mice. Horse IgG agglutinated human type O+ erythrocytes, whereas no such reactivity was observed in sheep and camel IgG preparations. A novel procedure was used for the detection of antibodies in human serum against animal IgGs. It was found that a pool of human sera collected in Costa Rica had a higher titer of antibodies directed against horse and sheep IgGs than against camel IgG. Overall, camel IgG showed the lowest potential for the induction of adverse reactions among the three IgGs tested.
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Authors
MarÃa Herrera, Guillermo León, Alvaro Segura, Fabricio Meneses, Bruno Lomonte, Jean Philippe Chippaux, José MarÃa Gutiérrez,