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Specialty

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.
From Wikipedia, the free encyclopedia

Specialty

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.

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