Related Experiment Video
Updated: Jul 21, 2026
Capillary Electrophoresis Separation of Monoclonal Antibody Isoforms Using a Neutral Capillary
Published on: January 16, 2017
Peptide mapping characterization by capillary electrophoresis of a human monoclonal anti-Rh(D) antibody produced for
N Bihoreau1, C Ramon, R Vincentelli
1Department of Analytical Biochemistry, French Laboratory of Fractionation and Biotechnology, Les Ulis, France.
CE has been employed for peptide mapping characterization of the light chain of a human anti-Rhesus (D) (Rh[D]) antibody presently undergoing clinical evaluation. In the presence of an ion-pairing agent used to increase resolution, reproducible maps were obtained within 55 min after injection of 12 fmol of protein. CE has also been employed as a direct and quick screening tool for purity evaluation of the tryptic peptides obtained from reversed-phase high-performance liquid chromatography (RP-HPLC) prior to sequence analysis. Post-translational modifications of the protein were determined by identification of the cysteine residues implicated in disulfide linkages.
CE has been employed for peptide mapping characterization of the light chain of a human anti-Rhesus (D) (Rh[D]) antibody presently undergoing clinical evaluation. In the presence of an ion-pairing agent used to increase resolution, reproducible maps were obtained within 55 min after injection of 12 fmol of protein. CE has also been employed as a direct and quick screening tool for purity evaluation of the tryptic peptides obtained from reversed-phase high-performance liquid chromatography (RP-HPLC) prior to sequence analysis. Post-translational modifications of the protein were determined by identification of the cysteine residues implicated in disulfide linkages.
