Post-translational structural modifications of immunoglobulin G and their effect on biological activity

The size, heterogeneity, and biological production process of protein therapeutics like monoclonal antibodies create unique challenges for their analysis and regulation compared with small molecules. Complete structural characterization of a molecule 1000-fold heavier than aspirin is no small feat....

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Veröffentlicht in:	Analytical and bioanalytical chemistry 2015, Vol.407 (1), p.79-94
Hauptverfasser:	Hmiel, Laura K., Brorson, Kurt A., Boyne, Michael T.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analysis Analytical Chemistry Animals Antibodies Biochemistry Biological Characterization and Evaluation of Materials Chemistry Chemistry and Materials Science Control Food Science Glycosylation Heterogeneity Humans Immunoglobulin G Immunoglobulin G - chemistry Immunoglobulin G - genetics Immunoglobulin G - metabolism Immunoglobulin G - therapeutic use Immunoglobulins Laboratory Medicine Mathematical analysis Monitoring/Environmental Analysis Monoclonal antibodies Protein Processing, Post-Translational Proteins Review Strategy
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