General Ligand Affinity Chromatography in Enzyme Purification Ligands, Affinity Chromatography, Enzyme Purification

Publisher Website
Google Scholar
Abstract
Recent developments in enzyme purification have revolutionized isolation techniques and at the same time provided a more profitable manner in which to obtain them. These developments are primarily concerned with the preparation and usability of imobilized ligands for the selective isolation and purification of biologically active substance1–5, particularly enzymes. This technique is based on the unique principle that the biological macromolecule is able to be adsorbed to the immobilized ligand, specifically and reversibly, unlike the traditional methods by which proteins are separated by their dffferences in physicochemical properties. Numerous proteins have been purified since this technique was first applied by Campbell et al.6 for the purification and isolation of antibodies. From these preliminary efforts it is apparent that further development of thfs method would greatly facilitate our understanding and utilizattion of enzymes.