title: Purification of Trichinella spiralis tubulin: comparison of several analytic procedures.
abstract: 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%.
authors.affiliation: Department of Microbiology and Parasitology, Faculty of Pharmacy, University of Alcala, Madrid, Spain. mpperez@microb.alcala.es
authors.forename: J
authors.initials: J
authors.lastname: Martínez González
authors.forename: A
authors.initials: A
authors.lastname: Jiménez González
authors.forename: F
authors.initials: F
authors.lastname: Rodríguez Caabeiro
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D017160:Trichinella spiralis / Q000737:chemistry*; D014404:Tubulin / Q000276:immunology / Q000302:isolation & purification*
chemical_list: D000911:Antibodies, Monoclonal; D014404:Tubulin