Purification of Trichinella spiralis tubulin: comparison of several analytic procedures.

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-alpha and anti-beta-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%.