Abstract
The outer part ofHymenolepis diminuta tegument was extracted with 3m KCl. The antigen was adsorbed from the extract on an affinity column containingH. diminuta-infected rat immunoglobulin immobilized on Sepharose 4B and could be eluted with 2.5m urea at pH 2.8. Analysis of polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of both the crude extract and material eluted from the column showed that the latter was markedly purified. Double diffusion and immunoelectrophoresis revealed 11 and 4 antigenic components in the crude extract and purified preparation, respectively.
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Krawczuk, S., Rode, W. & Machnicka, B. Purification and immunologic reactivity ofHymenolepis diminuta surface antigens. Parasitol Res 76, 707–711 (1990). https://doi.org/10.1007/BF00931091
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DOI: https://doi.org/10.1007/BF00931091