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Biophysical Characterization of a Therapeutic mAb and its Associated Antigen-Binding Fragments

Summary: Changes during purification, formulation, fill-finish, and distribution can affect protein stability and practically all steps in the manufacturing process may perturb the higher-order structure and heterogeneity of the molecule, thus determining size homogeneity of a monoclonal antibody in solution is important for comparability and characterization of these medications. For this study, an IgG antibody was cleaved into antigen-binding fragments using pepsin and papain digestion, followed by protein purification. The fragments, along with intact mAb, were studied by Sedimentation Velocity-Analytical Ultracentrifugation (SV-AUC) and Size-Exclusion Chromatography Multi-Angle Light Scattering (SEC-MALS) to determine sedimentation coefficient, distribution, and molecular weight of each. 

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