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  • Title: Bound and unbound pyridine dinucleotides in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes.
    Author: Canepa L, Ferraris AM, Miglino M, Gaetani GF.
    Journal: Biochim Biophys Acta; 1991 May 24; 1074(1):101-4. PubMed ID: 2043659.
    Abstract:
    We have measured, by a sensitive cycling assay, the concentration of bound and unbound dinucleotides in normal and glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes. Measurement of free NADP in ultrafiltrates confirms that in normal erythrocytes almost all NADP is bound to cytosolic proteins. In glucose-6-phosphate dehydrogenase-deficient erythrocytes unbound NADP is significantly higher than in normal red cells and the NADP+/NADPH ratio is largely in favor of the oxidized form. In normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes essentially all NAD (bound and unbound) is in the oxidized state. About 50% of the total amount of NAD (NAD+ + NADH) is free in the cytosol, with a NAD+/NADH ratio greater than 100.
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