Removal of sodium dodecyl sulphate from proteins isolated by sodium dodecyl sulphate polyacrylamide gel electrophoresis
- 1 March 1990
- journal article
- research article
- Published by Wiley in Biomedical Chromatography
- Vol. 4 (2) , 89-90
- https://doi.org/10.1002/bmc.1130040212
Abstract
A procedure is described for the removal of sodium dodecyl sulphate (SDS) from proteins isolated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The proteins separated by SDS-PAGE were stained with Coomassie Blue and extracted with Tris-HCI buffer containing SDS. The obtained extracts were subjected to gel permeation chromatography in an acidic aqueous acetonitrile solution. The procedure allows purification of the isolated proteins not only from SDS, but also from Coomassie Blue, buffer salts and other small molecular weight contaminants.Keywords
This publication has 6 references indexed in Scilit:
- Preparative fractionation of amyloid proteins on a microgram scale by high-performance liquid chromatography and polyacrylamide gel electrophoresisClinica Chimica Acta; International Journal of Clinical Chemistry, 1987
- Removal of sodium dodecyl sulphate from proteins by gel permeation chromatographyJournal of Chromatography B: Biomedical Sciences and Applications, 1987
- Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: Results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymesAnalytical Biochemistry, 1980
- Spectrophotometric measurement of dodecyl sulfate with basic fuchsinAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951