Journal of Liquid ChromatographyPublication details, including instructions for authors and subscription information:
ABSTRACTThe use of high ionic strength buffers with capillary electrophoresis in untreated fused silica capillaries is demonstrated for the separation of proteins and peptides. Short, small i.d. (20-25 pm) capillaries are useful as a quick screening tool for protein analysis. Electropherograms of standard proteins run from pH 5.0 to 10.0 in 0.5 M sodium phosphate buffers suggest that at these high ionic strengths, the proteins (relative to the electrmmotic flow markers) are not always predictable functions of their PI'S. Consecutive runs of standard proteins yield excellent migration time and peak area reproducibility. Milk proteins, particularly the caseins, could be separated with the addition of 4 M urea to the buffer. Alternatively, the addition of a zwitterion to a phosphate-based buffer provide different selectivities for the protein standards. The accompanying reduction in ionic strength allows for
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