Aggregation and pH–temperature phase behavior for aggregates of an IgG2 antibody
✍ Scribed by Erinc Sahin; William F. Weiss IV; Andrew M. Kroetsch; Kevin R. King; R. Kendall Kessler; Tapan K. Das; Christopher J. Roberts
- Book ID
- 112134456
- Publisher
- John Wiley and Sons
- Year
- 2012
- Tongue
- English
- Weight
- 342 KB
- Volume
- 101
- Category
- Article
- ISSN
- 0022-3549
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Two major aggregation pathways observed in an IgG2 molecule are described. Different aggregate species generated by long-term incubation of the antibody at 37 degrees C were collected by a semi-preparative size exclusion chromatography method. These purified species were analyzed extensively by dena
Changes in protein-protein interactions, protein unfolding, and nonnative aggregation were assessed for a series of human IgG1 antibodies as a function of pH and solution ionic strength (I). Unfolding transitions were characterized with differential scanning calorimetry. Protein-protein interactions
Monomeric and aggregated states of an IgG1 antibody were characterized under acidic conditions as a function of solution pH (3.5-5.5). A combination of intrinsic/extrinsic fluorescence (FL), circular dichroism, calorimetry, chromatography, capillary electrophoresis, and laser light scattering were u