Purification of recombinant proteins can be regarded as the most frequent application of affinity chromatography (Melander et al. 1999). The proteins in question may have been passed through genetic modification to allow optimum selection for affinity binding. In this case, the proteins are referred to as â€œfusion proteinsâ€ (Mattiasson et al. 1999). Various types of tags are available for use; the most common types include â€œglutathione-S-transferase (GST), hexahistidine (his), and maltose-binding protein (MBP)â€ (Melander et al. 1999). The tags are often used in the elution process. For instance, â€œthe GST has an affinity for glutathione which is commercially available as immobilized glutathione agaroseâ€ (Mattiasson et al. 1999). During the elution process, excess glutathione is used to displace the tagged protein.
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