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- W2023412792 abstract "1. A new variant of human erythrocyte glucosc-6-phosphate dehydrogenase is described, with approximately 1 per cent normal activity. 2. The enzyme differs from the normal enzyme in being very thermolabile, having a biphasic pH activity profile and reduced Michaelis constant for glucose-6-phosphate (8.5 μM). 3. The Michaelis constant of the variant enzyme for glucose-6-phosphate (G6P) at infinite NADP concentration is also lower (7.3 μM) than that of the normal (19.3 μM), whilst the dissociation and Michaelis constants for NADP are comparable to those for the normal enzyme. 4. The utilization by the variant enzyme of 2-deoxy-G6P was found to be 30 per cent of G6P utilization, as compared to 4 per cent for the normal enzyme. This was shown to be due to a lower Km, of the variant enzyme for 2-deoxy-G6P. 5. Electrophoretic mobility is slower than normal. 6. This variant appears differ from all previously reported variants, and it is proposed to call it G6PD Port Elizabeth." @default.
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- W2023412792 date "1973-01-01" @default.
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- W2023412792 title "A new variant of human erythrocyte glucose-6-phosphate dehydrogenase: G6PD port Elizabeth" @default.
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- W2023412792 doi "https://doi.org/10.1016/0020-711x(73)90045-1" @default.
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