Purification and properties of adenosine 5′-triphosphate-d-glucose 6-phosphotransferase from rat liver

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Abstract
An 870-fold purification of glucokinase from rat liver is described which involves (NH4)2SO4 fractionation and the use of DEAE [diethylaminoethyl] Sephaaex, DEAE-cellulose and polyacrylamide columns. The preparation is free of any interfering enzymes and has a specific activity of 8 [mu]moles/min./mg of protein. Glucokinase catalyses the phosphory-lation of glucose, mannose and 2-deoxyglucose. The enzyme is inhibited by high concentrations of glucose 6-phosphate only; adenosine diphosphate is an inhibitor whose effect depends on the Mg2+ concentration. The properties of glucokinase are compared briefly with those of other phosphotransferases.