Abstract
Affinity chromatography is based on the highly selective interaction between an immobilized ligand and a particular structural element on the target biomolecule, usually a protein. The term affinity chromatography was initially reserved for functional biological interactions only (e.g., antibody-antigen, lectin-glycoprotein, and enzyme-inhibitor). The term is now used more freely to include any interaction that is due to the occurrence of specific groups on the target surface, e.g., the interaction between an oligo-histidine motif and a chelated metal ion (immobilized metal ion affinity chromatography, IMAC). These types of ligands are sometimes referred to as pseudo-biospecific affinity, and there is not a clear distinction between them and multimodal chromatography ligands.
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