Peptide mapping characterization by capillary electrophoresis of a human monoclonal anti-Rh(D) antibody produced for clinical study.
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.
Bihoreau
N
N
Department of Analytical Biochemistry, French Laboratory of Fractionation and Biotechnology, Les Ulis, France.
Ramon
C
C
Vincentelli
R
R
Levillain
J P
JP
Troalen
F
F
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000032:analysis* / Q000737:chemistry / Q000276:immunology; D019075:Electrophoresis, Capillary; D006801:Humans; D008969:Molecular Sequence Data; D010449:Peptide Mapping / Q000379:methods*; D012204:Rh-Hr Blood-Group System / Q000276:immunology*
D000911:Antibodies, Monoclonal; D012204:Rh-Hr Blood-Group System