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Analysis of mouse, rat, dog, marmoset, and human serum proteins by capillary electrophoresis: comparison with agarose gel electrophoresis
Author(s) -
Crivellente Federica,
Bonato Monica,
Cristofori Patrizia
Publication year - 2008
Publication title -
veterinary clinical pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 51
eISSN - 1939-165X
pISSN - 0275-6382
DOI - 10.1111/j.1939-165x.2008.00008.x
Subject(s) - capillary electrophoresis , agarose gel electrophoresis , agarose , blood proteins , electrophoresis , chromatography , serum protein electrophoresis , marmoset , reproducibility , microbiology and biotechnology , gel electrophoresis of proteins , biology , gel electrophoresis , quantitative analysis (chemistry) , chemistry , andrology , polyacrylamide gel electrophoresis , medicine , immunology , endocrinology , biochemistry , antibody , dna , paleontology , monoclonal , monoclonal antibody , enzyme
Background: Serum protein analysis in both humans and experimental animal species has so far been carried out by labor‐intensive techniques, such as agarose gel electrophoresis (AGE). Objective: The objective of this study was to evaluate capillary electrophoresis (CE) as an alternative technique to AGE for the analysis of serum proteins from healthy animals. Methods: Blood samples were collected into tubes without anticoagulant from 6 fasted healthy male mice, rats, dogs, marmosets, and humans. Serum proteins were separated by CE using a technique standardized for the analysis of human proteins, and the results (efficiency, resolution, and precision) were compared with those obtained through AGE. Results: Compared with AGE, CE resulted in narrower peaks and more peaks. The efficiency of protein separation by CE was significantly higher for all species, and resolution ( R ) was significantly higher in samples from dogs. Using rat serum, intraday reproducibility was lower for all protein fractions, and interday reproducibility was lower for most peaks, compared with AGE. Conclusions: We conclude that CE is a viable alternative to AGE for the determination of protein electrophoresis in a routine veterinary clinical pathology laboratory. The minimal sample requirement (2 μL), complete automation, and quantitative results make CE an especially valuable technique for protein analysis in experimental animal models.