ABSTRACT
The complexes formed between a protein (bovine serum albumin, BSA) and a surfactant (sodium dodecyl sulfate, SDS) were studied as separation carriers in electrokinetic chromatography. Selectivities different from those with either SDS or BSA alone in the background electrolyte (BGE) were obtained. Separation performances were demonstrated to be closely related to the type of complex formed, as predicted by the isotherm curve of SDS on BSA. For each composition of background electrolyte, capacity factors and resolutions were calculated. We compared the results with these complexes to electropherograms using BGE containing either BSA or SDS alone. The separation of a mixture of phenols indicate that some compositions of the BSA-SDS complexes are efficient selectors.
