This review article with 223 references describes recent developments in capillary electrophoresis (CE) of proteins and covers papers published during last two years, from the previous review (V. Dolnik, Electrophoresis 1999, 20, 3106-3115) through Spring 2001. It describes the topics related to CE of proteins including modeling of the electrophoretic properties of proteins, sample pretreatment, wall coatings, improving selectivity, detection, special electrophoretic techniques, and applications.

Capillary electrophoresis of proteins 1999–2001

In this paper, capillary electrophoresis in clinical and forensic analysis is reviewed on the basis of the literature of 1999, 2000 and the first papers in 2001. An overview of progress and relevant examples for each major field of application, namely (i) analysis of drug seizures, explosives residues, gunshot residues and inks, (ii) monitoring of drugs, endogenous small molecules and ions in biofluids and tissues, (iii) general screening for serum proteins and analysis of specific proteins (carbohydrate deficient transferrin, α1-antitrypsin, lipoproteins and hemoglobins) in biological fluids, and (iv) analysis of nucleic acids and oligonucleotides in biological samples, including oligonucleotide therapeutics, are presented.

Advances of capillary electrophoresis in clinical and forensic analysis (1999–2000)

La pèrdua del domini tecnològic en el laboratori clínic: transcendència estratègica i econòmica

Background: We evaluated a new, automated multicapillary zone electrophoresis (CE) instrument (Capillarys®, 4.51 software version; Sebia) for human serum protein analysis.

Methods: With the Capillarys β1-β2+® reagent set, proteins were separated at 7 kV for 4 min in 15.5 cm × 25 μm fused-silica capillaries (n = 8) at 35.5 °C in a pH 10 buffer with online detection at 200 nm. Serum samples with different electrophoretic patterns (n = 265) or potential interference (n = 69) were analyzed and compared with agarose gel electrophoresis (AGE; Hydrasys®-Hyrys®, Hydragel protein(e) 15/30® reagent set; Sebia).

Results: CVs were <3.5% for albumin, <11% for α1-globulin, <4.1% for α2-globulin, <7.4% for β-globulin, and <5.8% for γ-globulin (3 control levels); measured throughput was 60 samples/h. In patients without paraprotein (n = 116), the median differences between CE and AGE were −5.4 g/L for albumin, 4.0 g/L for α1-globulin, 0.7 g/L for α2-globulin, 0.6 g/L for β-globulin ( P <0.001 for all fractions), and −0.1 g/L for γ-globulin (not significant). More samples had at least one γ-migrating peak detected by CE (n = 135 vs 130; paraprotein detection limit, ∼0.5–0.7 g/L), but fewer were quantified (n = 84 vs 91) because of γ- to β-migration shifts. There was a 1.2 g/L median difference between CE and AGE for γ-migrating paraprotein quantification (n = 69; P <0.001). Several ultraviolet-absorbing substances (lipid emulsion, hemoglobin) or molecules (contrast agent, gelatin-based plasma substitute) induced CE artifacts.

Conclusions: The Capillarys instrument is a reliable CE system for serum protein analysis, combining advantages of full automation (ease of use, bar-code identification, computer-assisted correction of α1-globulins) with high analytical performances and throughput.

/pdf/automated-multicapillary-electrophoresis-for-analysis-of-28l606j55b.pdf

Automated Multicapillary Electrophoresis for Analysis of Human Serum Proteins

Purpose: Accurate classification of menopausal status is important to epidemiological research evaluating the role of reproductive hormones in disease processes. Algorithms relying on repeat hormone assays are unfeasible in large epidemiological studies. This paper summarizes the development of the Women's Ischemia Syndrome Evaluation (WISE) Hormonal menopausal status algorithm for determining premenopausal, perimenopausal, and postmenopausal status using menstrual and reproductive history and reproductive hormone levels obtained at a single clinic visit. Methods: The authors compared the accuracy of this algorithm with two currently used selfreport algorithms: Menstrual, based only on months since last menstrual period, and Historical, which adds age and surgical history. Results: The study population consisted of 515 women (329 clearly postmenopausal) enrolled in the WISE study who were undergoing coronary angiography for suspected ischemia. A subgroup of 186, not clearly postmenopausal, was classified ...

Determination of menopausal status in women: the NHLBI-sponsored Women's Ischemia Syndrome Evaluation (WISE) Study.

The detection and quantification of monoclonal free light chains in urine (Bence Jones protein, BJP) are thorny issues for the laboratorian. Immunoelectrophoretic techniques (immunofixation) allow the characterization of the two pathognomonic features of light chains: monoclonality and absence of heavy chains. Immunochemical methods such as nephelometry and turbidimetry are widely used in clinical practice to exclude the presence of BJP. However, these methods are limited by several metabolic and analytical problems. The accuracy of quantitative immunochemical methods is hampered by the heterogeneous molecular forms (fragments and polymers) of BJP and by the lack of reference materials, and the precision of the methods in clinically relevant regions of the dynamic range is poorly defined. Immunoelectrophoretic methods, especially immunofixation, are recommended because of their ability to demonstrate monoclonality and the absence of heavy chains. Immunofixation is also considered the best method to document the disappearance of the monoclonal protein (complete remission). The physiology of immunoglobulins and the clinical relevance of BJP are illustrated in the two appendices to this paper.

Guidelines for the analysis of Bence Jones protein.

The Paragon CZE 2000 (Beckman Analytical, Milan, Italy) is an automatic dedicated capillary zone electrophoresis (CZE) system, producing a five-zone serum protein pattern with quantitative estimation of the zones. With the view of substituting this instrument for two previously used serum protein electrophoresis techniques, we planned to produce reference values for the "new" systems leading to compatible interpretation of the results. High resolution cellulose acetate electrophoresis with visual inspection and descriptive reporting (HR-CAE) and five-zone cellulose acetate electrophoresis with densitometry (CAE-D) were the previously used techniques. Serum samples (n = 167) giving "normal pattern" with HR-CAE were assayed with the CZE system, and the results were statistically assessed to yield 0.95 reference intervals. One thousand normal and pathological serum samples were then assayed with the CAE-D and the CZE techniques, and the regression equations of the CAE-D values over the CZE values for the five zones were used to transform the CAE-D reference limits into the CZE reference limits. The two sets of reference values thereby produced were in good agreement with each other and also with reference values previously reported for the CZE system. Thus, reference values for the CZE techniques permit interpretation of results coherent with the previously used techniques and reporting modes.

Serum proteins by capillary zone electrophoresis: approaches to the definition of reference values.

Electrophoresis: cellulose acetate vs agarose gel, visual inspection vs densitometry.

Serum protein analysis by molecular interpretation of cellulose acetate electrophoresis: evaluation of its clinical usefulness

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Guidelines for the analysis of Bence Jones protein.

Serum proteins by capillary zone electrophoresis: approaches to the definition of reference values.

Electrophoresis: cellulose acetate vs agarose gel, visual inspection vs densitometry.

Serum protein analysis by molecular interpretation of cellulose acetate electrophoresis: evaluation of its clinical usefulness