Pseudo-affinity chromatography

Interaction with ligands Metal binding Pseudo-affinity chromatography Immobilized metal ion affinity chromatography (IMAC)... 

Ion-exchange, hydrophobic-interaction chromatography chromatography on hydroxyapatite and different types of affinity and pseudo-affinity chromatography are the most frequently used methods for isolation of nondenatured, physiologically active proteins. 

Affinity chromatography (AC) is a fractionation technique widely used in targeted proteomics or protein-protein interaction approaches. This method utilizes an interaction or affinity of a target protein to a substrate (or another protein) immobilized on a support matrix. Figure 17.4 demonstrates that AC can be incorporated into 3D proteomic approaches (Lee and Lee, 2004). Traditionally, AC has been used to purify, for example, carbohydratebinding proteins from Diplostomum pseudo-spathaceum (Mikes and Man, 2003) and the detoxification superfamily glutathione transferase (GST) from parasitic flatworms (Brophy and Barrett, 1990), specifically shown in... 

Since no biospecific interactions are characteristic of affinity separations, immobihzed metal-affinity chromatography) and chromatography on synthetic dye hgands are usually called pseudo-affinity techniques. 

Isolation of prolactin by immunoadsorption Isolation of a pseudo-Tamm-Horsfall glycoprotein by affinity chromatography Isolation of a pseudo-Tamm-Horsfall glycoprotein by affinity chromatography Immunoadsorption of anti-(blood-group A substance) antibody... 

Tanaka, Y, and Terabe, S. (1995). Partial separation zone technique for the separation of enantiomers by affinity electrokinetic chromatography with proteins as chiral pseudo-stationary phases. J. Chromatogr. A 694, 277—284. 

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