A chromatographic technique that exploits specific biological interactions to separate molecules, using a stationary phase with ligands that selectively bind target molecules. Only molecules with affinity for the immobilized ligand are retained and can be specifically eluted.
Named for the specific 'affinity' (binding attraction) between the target molecule and immobilized ligand, combined with 'chromatography.' Developed in the 1960s by Pedro Cuatrecasas and Christian Anfinsen, revolutionizing protein purification by exploiting biological recognition.
Affinity chromatography is like molecular fishing with the perfect bait - it can pluck one specific protein out of thousands by using its natural binding partner as a hook! It's so selective that you can purify a protein from a crude cell extract in a single step, something that might otherwise take dozens of purification steps.
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