Characterization of the glycosylation state of a recombinant monoclonal antibody using weak cation exchange chromatography and mass spectrometry
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概要
- 論文の詳細を見る
- 2008-02-01
著者
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Liu Hongcheng
Process Sciences Department Abbott Bioresearch Center
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Chumsae Chris
Process Sciences Department Abbott Bioresearch Center
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Gaza-bulseco Georgeen
Process Sciences Department Abbott Bioresearch Center
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Gaza-bulseco Georgeen
Protein Analytics Process Sciences Department 100 Research Drive Abbott Bioresearch Center
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BULSECO Ashley
Process Sciences Department Abbott Bioresearch Center
関連論文
- Comparison of methionine oxidation in thermal stability and chemically stressed samples of a fully human monoclonal antibody
- Characterization of the stability of a fully human monoclonal IgG after prolonged incubation at elevated temperature
- Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein A and protein G
- Characterization of the glycosylation state of a recombinant monoclonal antibody using weak cation exchange chromatography and mass spectrometry
- Assessment of antibody fragmentation by reversed-phase liquid chromatography and mass spectrometry
- Structural effect of a recombinant monoclonal antibody on hinge region peptide bond hydrolysis