eng URI http://hdl.handle.net/10795/2691 βιοχημεία ένζυμα Dye-ligand affinity chromatography is a widely used technique in protein purification. The utility of the reactive dyes as affinity ligands results from their unique chemistry, which confers wide specificity towards a large number of proteins. They are commercially available, are inexpensive, and can easily be immobilized. Important factors that contribute to the successful operation of a dye-ligand chromatography include adsorbent properties, such as matrix type and ligand concentration, the buffer conditions used in the adsorption and elution stages, and contacting parameters like flow rate and column geometry. In general, with dye-ligand affinity chromatography, the specificity is provided by the adsorption and elution conditions employed in a particular purification, and these must often be worked out by trial and error. The present chapter provides protocols for the synthesis of dye-ligand affinity adsorbents as well as protocols for screening, selection, and optimization of a dye-ligand purification step. The purification of the glutathione transferases from Phaseolus vulgaris crude extract on Cibacron Blue 3GA-Sepharose is given as an example. 14 pp. LOMv1.0 creator LOMv1.0 publisher LOMv1.0 Project Final Beneficiary LOMv1.0 Project Executing Organisation 2014 Digital Library of the Operational Programme "Education and Lifelong Learning" abstract types Text Affinity chromatography Cibacron Blue 3GA Dye-ligand chromatography Glutathione transferase Triazine dyes 2114567 application/pdf http://repository.edulll.gr/edulll/bitstream/10795/2691/2/2691_Document-23.pdf Editor's proof, uncorrected. URI http://hdl.handle.net/10795/2691 LOMv1.0creator 2016-04-15T13:00:19Z LOMv1.0validator 2016-04-15T13:00:19Z LOMv1.0 gre no no Copyright EYD-EPEDBM (Operational Programme "Education and Lifelong Learning")