Characterization of protein behavior in high-performance capillary electrophoresis using a novel capillary system.
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.
Swedberg
S A
SA
Hewlett-Packard Laboratories, Chemical Systems Department, Palo Alto, California 94303.
D004356:Drug Storage; D004586:Electrophoresis / Q000379:methods*; D005464:Fluorobenzenes; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D009994:Osmolar Concentration; D011506:Proteins / Q000032:analysis*; D015203:Reproducibility of Results
D005464:Fluorobenzenes; D011506:Proteins