Characterization of Site-Specific Glycation During Process Development of a Human Therapeutic Monoclonal Antibody

A therapeutic recombinant monoclonal antibody (mAb1) was found to be highly susceptible to glycation during production. Up to 42% glycation was observed in mAb1, which was significantly greater than the glycation observed in 17 other monoclonal antibodies (mAbs). The majority of the glycation was lo...

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Veröffentlicht in:	Journal of pharmaceutical sciences 2011-07, Vol.100 (7), p.2543-2550
Hauptverfasser:	Miller, Amanda K., Hambly, David M., Kerwin, Bruce A., Treuheit, Michael J., Gadgil, Himanshu S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence analytical biochemistry Antibodies, Monoclonal - biosynthesis Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - genetics Antibodies, Monoclonal - therapeutic use Biological and medical sciences biotechnology Buffers Cation Exchange Resins Chromatography, Ion Exchange Chromatography, Reverse-Phase Complementarity Determining Regions - metabolism General pharmacology Glucose - metabolism glycoprotein Glycosylation HPLC (high-performance/pressure liquid chromatography) Humans Hydrogen-Ion Concentration Immunoglobulin Heavy Chains - metabolism Kinetics Lysine macromolecular prodrugs mass spectrometry Medical sciences Mutagenesis, Site-Directed Mutation Peptide Mapping Pharmaceutical technology. Pharmaceutical industry Pharmacology. Drug treatments Protein Processing, Post-Translational Protein Structure, Secondary proteins Recombinant Proteins - biosynthesis Spectrometry, Mass, Electrospray Ionization Structure-Activity Relationship Technology, Pharmaceutical - methods
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