Purification of monoclonal antibodies is one of the major applications of chromatography in the life sciences. Protein A and Protein G supports provide an efficient means to purify various classes of immunoglobulins. However, the species or subclass specificities, high costs, and relatively harsh elution conditions associated with such supports are often incompatible with the overall purification strategy. Potential leakage of Protein A or G from these supports can also be problematic for antibodies destined for therapeutic applications.
The recently introduced series of analytical and preparative Bio-Scale chromatography columns provides several options for the purification of immunoglobulins in a cost effective manner under gentle elution conditions. The methods detailed in this study for monoclonal antibody purification include:
- Tandem use of DEAE Affi-Gel® blue mixed mode anion exchange/dye ligand followed by Bio-Scale CHT-I ceramic hydroxyapatite chromatography column
- Cation exchange chromatography using a Bio-Scale S strong cation exchange column
- Anion exchange chromatography using a Bio-Scale DEAE weak anion exchange column
All three methods provide cost effective alternatives to affinity based methods for monoclonal antibody purification. The results, advantages, and disadvantages of the different methods are discussed in this study.