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- α and anti- β-tubulin fixed to activated Sepharosa 4B...

Full description

Saved in:
Bibliographic Details
Published in:Veterinary parasitology 1998-06, Vol.77 (2), p.115-121
Main Authors: Gonzalez, J.M. (Alcala de Henares Univ., Madrid (Spain). Faculty of Pharmacology, Dept. of Microbiology and Parasitology), Gonzalez, A.J, Caabeiro, F.R
Format: Article
Language:English
Subjects:
Animals
Antibodies, Monoclonal - immunology
Chromatography, Affinity
Chromatography, Ion Exchange
ELECTROFORESIS
ELECTROPHORESE
ELECTROPHORESIS
Electrophoresis, Polyacrylamide Gel
PROTEINAS
PROTEINE
PROTEINS
PURIFICACION
PURIFICATION
TRICHINELLA SPIRALIS
Trichinella spiralis - chemistry
Tubulin
Tubulin - immunology
Tubulin - isolation & purification
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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%.
ISSN:0304-4017
1873-2550
DOI:10.1016/S0304-4017(98)00098-3