[A comparative study of the interaction between glutathione reductase and 6-phosphogluconate dehydrogenase of rat liver with certain affinity sorbents].

A comparative study of the conditions of interaction of some group-specific ligands with rat hepatic 6-phosphogluconate dehydrogenase and glutathione reductase was accomplished. The influence of ionic strength and coenzyme concentration in buffer solution on the extent of enzymes binding with immobilized 2',5'-ADP and procion red HE-3B was studied according to the residual enzymatic activity after the interaction of enzyme and adsorbent. The optimal conditions have been found for enzymes binding and for their elution resulted in the effective purification of the enzymes mentioned above. Enzymatic preparations were free from the contaminating activity of each other. Dye-ligand chromatography step on red sepharose was introduced into the three step scheme of the purification of 6-phosphogluconate dehydrogenase. The final preparation of 6-phosphogluconate dehydrogenase obtained by gradient salt elution of the enzyme from the red sepharose column (0-0.15 M KCl) has the specific activity of 30-34 E/mg and shows electrophoretical homogeneity. The contribution of ionic strength and biospecific interaction of the nucleotide binding site of the enzymes during chromatography on these adsorbents is discussed.