Abstract
The main principles and fields of application of a new method of enzyme chromatography, the so called "affinity" chromatography, are discussed. The method is based on the employment of an insoluble ligand of the enzyme (substrate, inhibitor, cofactor, etc.), that is sorption takes place owing to specific forces associated with affinities which constitute the basis of the biological function of the enzyme. The use of sorbents based on such ligands permits a more selective and effective isolation of pure enzymes from various sources compared with the usual types of sorbents, for example ion-exchange resins. In addition the review considers certain other techniques employing the specific affinity of the enzyme for the ligand in enzyme chromatography. Affinity chromatography can also be used to fractionate the products of chemical modification of enzymes and to investigate the physicochemical properties of enzyme–ligand complexes.
The bibliography includes 144 references.