Purification and properties of adenosine 5'-triphospae-D-glucose 6-phosphotransferase from rat liver.
1. An 870-fold purification of glucokinase from rat liver is described which involves ammonium sulphate fractionation and the use of DEAE-Sephadex, DEAE-cellulose and polyacrylamide columns. 2. The preparation is free of any interfering enzymes and has a specific activity of 8mumoles/min./mg. of protein. 3. Glucokinase catalyses the phosphorylation of glucose, mannose and 2-deoxyglucose. 4. The enzyme is inhibited by high concentrations of glucose 6-phosphate only; ADP is an inhibitor whose effect depends on the Mg(2+) concentration. 5. The properties of glucokinase are compared briefly with those of other phosphotransferases.
D000227:Adenine Nucleotides; D000818:Animals; D002623:Chemistry Techniques, Analytical; D002850:Chromatography, Gel; D005941:Glucokinase / Q000378:metabolism*; D005947:Glucose; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008274:Magnesium; D008358:Mannose; D051381:Rats
D000227:Adenine Nucleotides; D005941:Glucokinase; D008274:Magnesium; D005947:Glucose; D008358:Mannose