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Conflicting results between electrophoresis methods of serum M‐proteins
Author(s) -
Wuyts Birgitte,
Bossuyt Xavier,
Verhoef Gregor,
Blanckaert Norbert,
Delanghe Joris R.
Publication year - 2004
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200305871
Subject(s) - capillary electrophoresis , electrophoresis , agarose gel electrophoresis , resolution (logic) , chemistry , microbiology and biotechnology , isoelectric focusing , serum protein electrophoresis , chromatography , agarose , isoelectric point , gel electrophoresis of proteins , high resolution , staining , monoclonal antibody , monoclonal , biology , antibody , polyacrylamide gel electrophoresis , biochemistry , immunology , enzyme , dna , genetics , remote sensing , artificial intelligence , computer science , geology
The quantification of monoclonal immunoglobulins by protein electrophoresis has been helpful in determining the prognosis for the patient. In a 65‐year old man with documented IgG λ monoclonal gammopathy, a discrepancy in the detection and quantification of this M‐protein was found when studied by four different electrophoretic methods. On a high‐resolution agarose method with acid violet staining a prominent peak was seen in the fast γ‐region. A lower resolution agarose method using an amido black staining showed a small mid‐γ restriction, and no spike was detected by high‐resolution or lower resolution capillary zone electrophoresis. The discrepancy was not attributable to a migration in the β‐region leading to masking by transferrin or C3 peak, incorrect separation on CZE due to a high isoelectric point (p I > 8.5) or pentamerization of IgM M‐proteins. Therefore, other causes for discrepancies should be investigated.