BIOT 206 |
| The use of sedimentation velocity analytical ultracentrifugation (SV-AUC) to characterize protein self association and size distribution has become widespread within the biotechnology industry. Unlike alternative techniques such as size exclusion chromatography (SEC), and polyacrylamide gel electrophoresis (PAGE), SV-AUC involves minimal matrix interactions and can be carried out in a wide variety of buffers. SV-AUC also provides much higher size distribution resolving power than light scattering techniques. However, diverse factors (molecule-, formulation-, instrument-, technique-, and software-related) make it unusually difficult to establish meaningful estimates of accuracy, precision, and detection/quantitation thresholds for the SV-AUC technique. This study describes a multi-pronged approach to this problem for a monoclonal antibody therapeutic, where data simulations and an experimental campaign were combined to uncover sources of variability and determine method capabilities. |
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Biophysical and Biomolecular Symposium: Protein Misfolding and Aggregation
8:00 AM-11:00 AM, Wednesday, 13 September 2006 Hilton San Francisco -- Yosemite B, Oral
Division of Biochemical Technology |