[Detection of a new anomalous variant of glucose-6-phosphate dehydrogenase in human erythrocytes].
Kinetic and electrophoretic properties of 230--300 fold purified preparations of glucose-6-phosphate dehydrogenase (G6PD) from red cells of donors and patients with acute drug hemolytic anemia due to G6PD deficiency were studied. A new abnormal variant of G6PD isolated from red cell of a patient with acute drug hemolytic anemia, which was not described in literature, has been discovered. The abnormal enzyme differs from the normal by decreased Michaelis constant for glucose-6-phosphate and nicotinamide adenine dinucleotide phosphate (NADP), by increased utilization of analogues of substrates--2-deoxy-glucose-6-phosphate and particularly deamino-NADP, by low thermal stability, by the character of pH-dependence, by the appearance of a single band of G6PD activity in polyacrylamide gel electrophoresis.
D002384:Catalysis; D003847:Deoxyglucose; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D005954:Glucosephosphate Dehydrogenase / Q000302:isolation & purification*; D005955:Glucosephosphate Dehydrogenase Deficiency / Q000201:enzymology*; D005958:Glucosephosphates; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009243:NAD / Q000031:analogs & derivatives
D005958:Glucosephosphates; D009243:NAD; D003847:Deoxyglucose; D005954:Glucosephosphate Dehydrogenase
Vyiavlenie novogo anomal'nogo varianta gliukozo-6-fosfatdegidrogenazy v éritrotsitakh cheloveka.