Characterization of protein behavior in high-performance capillary electrophoresis using a novel capillary system |
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Authors: | S A Swedberg |
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Affiliation: | Hewlett-Packard Laboratories, Chemical Systems Department, Palo Alto, California 94303. |
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Abstract: | Original calculations of over a million theoretical plate efficiency for macromolecular solutes in the open tubular high-performance capillary electrophoresis experiment considered axial diffusion to be the efficiency limiting factor. In practice, interactions of biopolymers, such as proteins, with the capillary wall has had a significant impact on readily achieving high efficiencies for a wide variety of proteins. This paper reports a capillary system in which protein-surface interactions have been minimized, resulting in high efficiencies (greater than or equal to 300,000 theoretical plates). This system allows the analysis of a set of protein standards over a wide pI range at neutral pH and moderate ionic strength. The characterization of the behavior of those protein standards in this capillary system is described. |
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