PEPTIDE-MAPPING CHARACTERIZATION BY ELECTROPHORESIS OF A HUMAN MONOCLONAL ANTI-RH(D) ANTIBODY PRODUCED FOR CLINICAL-STUDY

被引：0
作者：
BIHOREAU, N
RAMON, C
VINCENTELLI, R
LEVILLAIN, JP
TROALEN, F
机构：
[1] FRENCH LAB FRACT & BIOTECHNOL,DEPT ANALYT BIOCHEM,F-91958 LES ULIS,FRANCE
[2] INST GUSTAVE ROUSSY,MICROCHEM LAB,F-94805 VILLEJUIF,FRANCE
来源：
JOURNAL OF CAPILLARY ELECTROPHORESIS | 1995年 / 2卷 / 04期
关键词：
CAPILLARY ELECTROPHORESIS; PEPTIDE MAPPING; HUMAN ANTI-RH(D) MONOCLONAL ANTIBODY; AMINO ACID SEQUENCE ANALYSIS;
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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页码：197 / 202
页数：6
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