[Kinetic properties of partially purified glucosephosphate dehydrogenase of human erythrocytes].
Partially purified glucose-6-phosphate dehydrogenase was isolated from small amounts of human erythrocytes (15-20 ml). The Km value for glucose-6-phosphate was 35.0 +/- 3.0 micronM, the Km for NADP was 4.27 +/- 0.3 micronM. The optimal activity of the enzyme was at pH 9.0. Glucose-6-phosphate dehydrogenase, dialyzed in presence of 1-10(-5) M NADP, had critical temperature about 52 degrees within 10 min of incubation; without NADP it was at 45 degrees. The method for isolation and purification of the enzyme was modified.
D000328:Adult; D002848:Chromatography, DEAE-Cellulose; D004912:Erythrocytes / Q000201:enzymology*; D005954:Glucosephosphate Dehydrogenase / Q000032:analysis / Q000097:blood* / Q000302:isolation & purification; D005958:Glucosephosphates / Q000032:analysis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008875:Middle Aged; D009249:NADP / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013696:Temperature
D005958:Glucosephosphates; D012965:Sodium Chloride; D009249:NADP; D005954:Glucosephosphate Dehydrogenase
Kineticheskie svoĭstva chastichno ochishchennoĭ gliukozo-6-fosfatdegisrogenazy eritrotsitov cheloveka