Separation of Intact Monoclonal Antibody Sialylation Isoforms by pH Gradient Ion Exchange Chromatography

摘要：

　　Glycosylated proteins,including erythropoietins,monoclonal antibodies,various hormones,constitute major approved therapeutic biological drugs.Sialic acid is important to cell recognition and migration and critical to circulation half life of the protein as exampled by therapeutic protein rhEPO.Thus monitoring protein glycosylation,including sialylation,is important for both glycoprotein characterization and quality control purposes.Standard oligosaccharide profiling (both fluorescently labeled and unlabeled) requires releasing the glycan from the protein and thus is time and labor consuming.Capillary electrophoresis,currently available technique for intact protein sialylation profiling,may not provide enough resolution.Thus an analysis method with both convenience and higher resolution is needed for protein sialylation monitoring.

作者: Dai Zhenyu Xu Qun Lina Liang Jeffrey Rohrer

作者单位: Chromatography and Mass Spectrometry Division,Thermo Fisher Scientific

会议类型: 国内会议

会议名称: 第十届全国生物医药色谱及相关技术学术交流会

会议地点: 威海

会议语种:英文

页码: 165-166

在线出版日期: 2014-04-19（万方平台首次上网日期，不代表论文的发表时间）