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Detection of specific bovine serum albumin‐sodium n‐dodecyl sulphate complexes by polyacrylamide gel electrophoresis
Author(s) -
DominguezReboiras M.,
Jones M. N.
Publication year - 1982
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150030604
Subject(s) - bovine serum albumin , chemistry , chromatography , polyacrylamide gel electrophoresis , electrophoresis , pulmonary surfactant , gel electrophoresis of proteins , gel electrophoresis , sodium dodecyl sulfate , sodium , molecular weight size marker , serum albumin , capillary electrophoresis , biochemistry , enzyme , organic chemistry
Polyacrylamide gel electrophoresis has been adapted to investigate bovine serum albumin (BSA) at sub‐saturation concentration levels of sodium n‐dodecyl sulphate (SDS). Two specific complexes were detected which coexisted between SDS concentrations of 0.4 and 5 mM. The binding isotherm for SDS on BSA was determined under comparable conditions by equilibrium dialysis and used in conjunction with the electrophoretic data to determine the composition of the complexes. The complexes had the following stoichiometry, BSA (SDS) 5 and BSA (SDS) 36 , and closely resembled two of the three complexes that have been observed by moving boundary electrophoresis. The experiments indicate that the polyacrylamide gel electrophoresis (PAGE) technique when applied below surfactant saturation could be a useful tool in the study of protein‐surfactant interactions.