Capillary gel electrophoresis: separation of major erythrocyte membrane proteins.
A new separation method of human erythrocyte membrane proteins by sodium dodecyl sulfate capillary gel electrophoresis (SDS-CGE) is described. In this method, a replaceable gel matrix was used. Seven major erythrocyte membrane proteins, alpha-and beta-spectrin, ankyrin 2.1, band 3 (anion-exchanger), 4.1a and b, and 4.2 (pallidin), were separated and identified by SDS-CGE method. High reproducible migration times of these proteins (inter-assay coefficients of variation less than 2%), as well as quantification (inter-assay coefficients of variation less than 11%) were obtained. This new SDS-CGE method may provide important diagnostic evidence for hereditary spherocytosis. It can be a powerful diagnostic tool in place of SDS polyacrylamide gel electrophoresis for erythrocyte membrane protein analysis.
Lin
C
C
Department of Clinical Chemistry, Hôpital Erasme, Université Libre de Bruxelles, Brussels, Belgium.
Cotton
F
F
Boutique
C
C
Dhermy
D
D
Vertongen
F
F
Gulbis
B
B
D019075:Electrophoresis, Capillary / Q000379:methods*; D004910:Erythrocyte Membrane / Q000737:chemistry*; D006801:Humans; D008565:Membrane Proteins / Q000302:isolation & purification*; D015203:Reproducibility of Results
D008565:Membrane Proteins