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Analysis of γ‐globulin mobility on routine clinical CE equipment: Exploring its molecular basis and potential clinical utility
Author(s) -
Vanderschaeghe Dieter,
Debruyne Evi,
Van Vlierberghe Hans,
Callewaert Nico,
Delanghe Joris
Publication year - 2009
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.200900054
Subject(s) - globulin , antibody , glycosylation , immunoelectrophoresis , electrophoresis , glycan , gamma globulin , chemistry , blood proteins , immunology , biochemistry , biology , glycoprotein
A study was conducted on the variability of γ‐globulin mobility in serum protein electrophoresis and its molecular basis. We found that the migration time of γ‐globulins can be reproducibly determined (CV=1.1%) on clinical CE equipment. Moreover, we found a significant difference ( p <0.001) in the migration of γ‐globulins between chronic liver disease patients ( n =98) and a healthy reference group ( n =47). Serum immunoglobulins were purified from these patients' sera using protein L ‐agarose and their glycosylation was studied using CE on a DNA sequencer. This glycomics approach revealed that several non‐sialylated N‐glycans show a moderate Pearson correlation coefficient ( r =0.2–0.4) with the migration time of γ‐globulins. Their sialylated structures correlate negatively ( r =−0.2 to −0.3). Immunoglobulins are significantly more sialylated in the healthy reference group compared with the patients ( p <0.001). We estimated that sialylation heterogeneity contributes about 36% to the molecular variance (carbohydrates and amino acid composition) that affects the electrophoretic mobility of immunoglobulins. This is the first report on the migration time of γ‐globulins on a clinical CE instrument and its potential clinical value to the routinely analyzed serum protein CE profiles.