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. 1978;19(1):69-75.
doi: 10.1016/0022-1759(78)90009-1.

Removal of unbound sodium dodecyl sulfate (SDS) from proteins in solution by electrophoresis through triton x-100-agarose

L T Lee, J E Deas, C Howe

Removal of unbound sodium dodecyl sulfate (SDS) from proteins in solution by electrophoresis through triton x-100-agarose

L T Lee et al. J Immunol Methods. 1978.

Abstract

Residual sodium dodecyl sulfate (SDS) introduces artifacts into immuno- and counterimmunoelectrophoretic analysis of proteins which have been eluted from preparative SDS-polyacrylamide gels. Unbound SDS can be removed by electrophoretic passage of eluted solutions through a barrier of Triton X-100 in agarose in which the anionic and non-ionic detergents interact to form micelles.

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