title: [[[Purification and properties of 6-phosphogluconate dehydrogenase from human erythrocytes].
abstract: 6-phosphogluconate dehydrogenase was purified from human erythrocytes by chromatography on 2'5' ADP Sepharose and ammonium sulfate precipitation, to a specific activity of 28 IU/mg of protein. The enzyme binds two NADP molecules per molecule of dimer with a Kd of 6.95 microM, or only one molecule of NADPH per molecule of dimer with a Kd of 0.38 microM. The substrate has no effect on the binding of NADPH, whereas increases the binding of a coenzyme analogue, the NADP oxidized with periodate. These findings indicate a possible regulatory role for 6-phosphogluconate dehydrogenase.
mesh_terms: D002846:Chromatography, Affinity; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D009249:NADP / Q000378:metabolism; D010734:Phosphogluconate Dehydrogenase / Q000097:blood / Q000302:isolation & purification*
chemical_list: D009249:NADP; D010734:Phosphogluconate Dehydrogenase
vernacular_title: Purificazione e proprietà della 6-fosfogluconato deidrogenasi da eritrociti umani.