Affinity chromatography bioaffinity

Enz)mies, inhibitors, cofactors, nucleic acids, hormones or cell chromatography can also be utilized as ligands in bioaffinity chromatography types. Examples of these methods include Receptor Affinity Chromatography and DNA Affinity Chromatography [21]. 

Enzyme purification was the first application of bioaffinity chromatography [23] and remains an important use of this technique. In this type of separation, ligands, such as enzyme inhibitors, coenzymes, or cofactors, are used to purify and separate enzymes [25]. For instance, in 1968 and the first report of "modem" affinity chromatography, Cuatrecasas, Wilchek, and Anfinsen employed specific enzyme inhibitors to selectively isolate enzymes [1,4]. A more recent example was the use of a support containing flavin mononucleotides for the purification of flavin adenine dinucleotide synthetase [26]. Other examples have included the use of mono-, di-, and triphosphate nucleotides for the purification of kinases and the use of nicotinamide adenine dinucleotide for the isolation of dehydrogenases [26,27]. 

Hage DS, Bian M, Burks R, Karle E, Ohnmacht C, Wa C. Bioaffinity chromatography. In Hage DS, editor. Handbook of affinity chromatography. 2nd ed. Boca Raton, FL CRC Press 2005. p. 101-26. 

Metal chelate and bioaffinity chromatography based on the affinity of the protein for a specific molecule that can be incorporated in the stationary phase (not commonly used for food analysis)... 

A widely applicable, non-chaotropic elution technique in bioaffinity chromatography is electrophoretic desorption [60,74,75]. If the affinant is coupled to the solid support by an azo bond or by thiol- or alcohol-ester bonds, the complex of the affinant with the isolated substance can be detached from the solid matrix and then the affinity ligand separated by dialysis or gel filtration. 

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