ABSTRACT
Protein A affinity chromatography has become well established as the preferred capture step for purification of human monoclonal IgG for in vivo applications, so much so that it has become largely regarded as generic. This has created the desire for an equally generic block of polishing methods to complete the purification. This chapter will discuss the suitability of anion exchange, cation exchange, hydrophobic interaction, and ceramic hydroxyapatite (CHT™ Bio-Rad) chromatography as candidates for this application. The strengths and limitations of each method will be discussed individually, and the merit of combining defined subsets with protein A toward the possibility of a generic overall IgG purification scheme will be considered.
