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This study compares the purity indices found after purifying tubulin obtained from the nematode parasite
Trichinella spiralis, using different chromatographic and electrophoretic methods. Affinity chromatography, using monoclonal antibodies anti-
α and anti-
β-tubulin fixed to activated Sepharosa 4B-CNBr, yields a tubulin purity of 15%. In contrast, by means of interchange-anionic chromatography using a column of DEAE-Sephadex-A50, we obtained an increase in purity of up to 75%. Finally, with the combined application of preparative electrophoresis and electroelution of proteins in polyacrylamide gels with SDS, we obtained the best results with a purity reaching 90%.