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- W1999754637 abstract "The tetrameric form of human erythrocyte glucose 6-phosphate dehydrogenase (G6PD) was investigated in respect to interaction of coenzyme at its ron-structural sites. 1:N6-ethenoadenine dinucleotide phosphate (ε-NADP), although displaying a lower catalytic efficiency compared to NADP, showed identical binding patterns, i.e. four moles per tetramer with a Kdiss of 1.0 μM. Furthermore, spectrofluorometric titrations with NADPH in the absence and in presence of varying NADP concentrations revealed a typically competitive mechanism of binding of NADP (four moles) and NADP (two moles) at the non-structural sites of the tetramer." @default.
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- W1999754637 title "Human erythrocyte glucose 6-phosphate dehydrogenase. Evidence for competitive binding of NADP and NADPH" @default.
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- W1999754637 doi "https://doi.org/10.1016/0006-291x(76)91090-1" @default.
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