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Capillary electrophoresis represents a relatively new analytical technique. This methodology has diversified and given rise to various modes such as capillary zone electrophoresis, capillary gel electrophoresis, micellar electrokinetic capillary chromatography, capillary isoelectric focusing and capillary isotachophoresis. If capillary electrophoresis was first introduced in research laboratories, this technique is now making an entrance to the clinical laboratory. This is due to its rapid and high-efficiency separation power, its potential applications and its possible automation. Thus, capillary electrophoresis represents an attractive alternative to some time-consuming techniques. Thanks to its versatility, the use of capillary electrophoresis has been proposed for the separation and quantification of a wide spectrum of biological components ranging from macromolecules (proteins, lipoproteins, nucleic acids) to small analytes (amino acids, organic acids or drugs). This paper illustrates the potential of capillary electrophoresis which should rapidly become a major technology for a modern clinical laboratory.

Serum protein electrophoresis and typing of monoclonal components (MCs) are routine but time-consuming and technically demanding assays. We evaluated capillary electrophoresis (Paragon CZE 2000) for automation of the two assays. CZE and cellulose acetate electrophoresis gave similar data on 794 samples. Within-run and between-run CVs were2% for albumin and gamma-globulins and 4-7% for alpha 1-, alpha 2-, and beta-globulins. Bilirubin, hemoglobin, triglycerides, and fibrinogen were found not to interfere. No carryover by capillaries was detected. The detection limit for MC was0.5 g/L. MC assessment by immunosubtraction on 403 samples identified the monoclonal type in all samples with peak concentrations10 g/L; only 50% of MCs that could not be quantified by densitometric scan were typed.