Purification of Antibodies by Affinity Chromatography

A ntibodies are becoming a dominant protein class for various human therapeutical applications and they represent the largest number of molecules in clinical trials today. Antibodies are purified using a combination of various purification techniques. The most popular technique is affinity chromatography based on specific interaction of immunoglobulin G (IgG) with affinity ligand. Affinity chromatography has several advantages since it is an easy, fast and selective procedure for capturing the target antibody. This review aims at describing different affinity techniques for purification of antibodies and reports the contributions of scientists working in this field and their important results. The main issues discussed in this review are: protein A affinity chromatography, histidine-ligand affinity chromatography, immobilized metal-chelate affinity chromatography, dye-ligand affinity chromatography, biomimetic affinity chromatography, negative chromatography, mixed-mode affinity chromatography, thiophilic chromatography, magnetically stabilized fluidized beds and aqueous two phase systems.