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It is a type of chromatographic lab technique used for purifying biological molecules within a mixture by exploiting molecular properties. Biological macromolecules such as enzymes and other proteins, interact with other molecules with high specificity through several different types of bonds and interaction. Such interactions including hydrogen bonding, ionic interaction, disulfide bridges, hydrophobic interaction, and more. The high selectivity of affinity chromatography is caused by allowing the desired molecule to interact with the stationary phase and become trapped within the column in order to be separated from the undesired material which will not interact and elute first.^[1]

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^ Ninfa, Alexander J.; Ballou, David P.; Benore, Marilee (2009). Fundamental Laboratory Approaches for Biochemistry and Biotechnology (2 ed.). Wiley. p. 133. ISBN 9780470087664.

[1] Ninfa, Alexander J.; Ballou, David P.; Benore, Marilee (2009). Fundamental Laboratory Approaches for Biochemistry and Biotechnology (2 ed.). Wiley. p. 133. ISBN 9780470087664.

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