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

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 i...

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Bibliographic Details
Published in:Journal of immunological methods Vol. 19; no. 1; p. 69
Main Authors: Lee, L T, Deas, J E, Howe, C
Format: Journal Article
Language:English
Published: Netherlands 1978
Subjects:
Counterimmunoelectrophoresis
Erythrocytes
Glycoproteins - analysis
Immunoelectrophoresis
Polyethylene Glycols
Proteins - analysis
Sepharose
Sodium Dodecyl Sulfate - isolation & purification
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Description
Summary: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.
ISSN:0022-1759
DOI:10.1016/0022-1759(78)90009-1