[Interaction of rat hepatic glucose-6-phosphate dehydrogenase with some group-specific immobilized ligands]

Conditions of the interaction of rat hepatic glucose-6-phosphate dehydrogenase and some group-specific adsorbents (2'5'-ADP-sepharose Cl-6B, Red sepharose CL-6B and Blue sepharose CL-6B) have been examined. The extent of this interaction was estimated according to such parameters as the volume of enzyme elution (Ve) and the recovery of the enzyme activity (%). The effect of the NADP concentration, values of pH and ionic strength of buffer solution on the parameters of enzyme binding with immobilized ligand was studied. The optimum conditions for the binding and specific elution of the enzyme were elucidated for each of the adsorbent studied. The scheme of glucose-6-phosphate dehydrogenase purification using the adsorbents studied is presented. It allows obtaining the preparation of the enzyme with specific activity about 100-240 U/mg and the extent of purification more than thousand fold.