-transparent.png){kind=logo}
Globular proteins, casein, and membrane proteins which were reacted with sodium dodecyl sulfate were studied by acid urea gel electrophoresis. The sodium dodecyl sulfate bound tightly to the proteins, producing a more acidic charge which prevented migration into the gel. When cetyltrimethylammonium bromide was added to the sodium dodecyl sulfate-protein complexes, the sodium dodecyl sulfate apparently reacted with cetyltrimethylammonium bromide and dissociated so that the proteins migrated in acid gel in a normal manner as compared to the proteins without any added detergent. The sodium dodecyl sulfate-cetyltrimethylammonium bromide complex could be removed from the proteins by centrifugation. Thus, cetyltrimethylammonium bromide used in conjunction with acid gel electrophoresis allows direct comparison by charge of proteins fractionated in the presence of sodium dodecyl sulfate with the starting mixture of proteins not exposed to detergent. The reaction of cetyltrimethylammonium bromide with sodium dodecyl sulfate in acidic urea also provides a simple convenient method of removal of sodium dodecyl sulfate from proteins.
J J Basch, and
H M Farrell
September 1994,
Analytical biochemistry,
J J Basch, and
H M Farrell
June 1994,
Molecular biotechnology,
J J Basch, and
H M Farrell
December 1993,
Electrophoresis,
J J Basch, and
H M Farrell
December 2021,
Cold Spring Harbor protocols,
J J Basch, and
H M Farrell
August 1996,
Electrophoresis,
J J Basch, and
H M Farrell
April 1995,
Electrophoresis,
J J Basch, and
H M Farrell
June 1992,
Electrophoresis,
J J Basch, and
H M Farrell
February 1975,
Journal of biochemistry,
J J Basch, and
H M Farrell
January 2022,
Gels (Basel, Switzerland),
J J Basch, and
H M Farrell
February 1994,
Electrophoresis,
