Abstract
Separations of model proteins obtained under denaturing conditions in the presence of micellar concentrations of ionic surfactants displayed high resolution and efficiency using either bare silica or C18-derivatized silica capillaries. Superior migration time reproducibility was achieved through the use of the C18-derivatized capillaries (run-to-run migration time % RSD = 0.2), relative to that obtained in bare silica capillaries (run-to-run migration time % RSD = 2.2), in the absence of buffer replenishment. The effects of surfactant concentration and pH upon the separation of a mixture of five model proteins of varying ionic and hydrophobic character were investigated, and the application of this technique to the analysis of a recombinant DNA-derived protein in fermentation broth was demonstrated.
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