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- W2007697410 abstract "A simple procedure, exploiting an affinity chromatography step on agarose-linked adenosine 2′,5′-bisphosphate, allows the concurrent purification from human red cell lysates of glucose 6-phosphate dehydrogenase (G6PD) and of another protein (FX). The latter, which has a higher electrophoretic mobility than G6PD, is not identifiable with any of a number of erythrocyte enzymes. It is a holoprotein, composed in its native form of two polypeptide chains of 33,000 Mr each and of one NADP equivalent. Native FX binds NADPH and this binding is competitive with NADP: The corresponding stoichiometry is 0.5 NADPH equivalents per 33,000 Mr (“half-site reactivity”), with a dissociation constant of 1 × 10−8m. On the basis of competition experiments, the dissociation constant for NADP is estimated to be 1.8 × 10−7m." @default.
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- W2007697410 title "Isolation and partial characterization of an NADP- and NADPH-binding protein from human erythrocytes" @default.
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- W2007697410 doi "https://doi.org/10.1016/0003-9861(77)90159-x" @default.
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