Abstract
A simple method for performing isoelectric focusing in uncoated and commercially available coated capillaries is described. Its main difference form other forms of CIEF is that electroosmotic flow (EOF) is not eliminated, but serves as the bulk flow to mobilize focused zones past a stationary detector. Separations of model protein mixtures in both uncoated and coated capillaries are shown. The coated capillary offers the best results in terms of separating both acidic and basic proteins, due to its constancy of EOF vs pH. The uncoated capillary can be used to successfully separate basic and neutral proteins. Limitations of the method in terms of nonlinear plots of migration time vs p l are addressed. The rigorous description of the experimental protocol that is given should allow performance of the technique on any commercial or home-made CE instrument.
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