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

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.