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Another use for affinity chromatography is the purification of specific proteins using a gel matrix that is unique to a specific protein. For example, the purification of E.Coli-B-Galactosidase is accomplished by affinity chromatography using P-Aminobenyl-1-Thio-B-D-Galactopyranosyl Agarose as the affinity matrix. P-Aminobenyl-1-Thio-B-D-Galactopyranosyl Agarose is used as the affinity matrix because it contains a galactopyranosyl group, which serves as a good substrate analog for E.Coli-B-Galactosidase. This property allows the enzyme to bind to the stationary phase of the affinity matrix and is eluted by adding increasing concentrations of salt to the column.[1]

  1. ^ Ninfa, Alexander J.; Ballou, David P.; Benore, Marilee (2009). Fundamental Laboratory Approaches for Biochemistry and Biotechnology (2 ed.). Wiley. p. 153.