Glucose-6-phosphate Dehydrogenase

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This chapter discusses glucose-6-phosphate dehydrogenase (G6P-DH), which was first isolated from erythrocytes and from fermenting yeast by Warburg et al., who carried out an extensive purification and characterization of the enzyme. Blood cells, adipose tissue, and lactating mammary gland are especially rich sources of the enzyme. Some human and animal tumors contain high activity of the enzyme. G6P-DH is applied in biochemistry and clinical chemistry. Triethanolamine buffer (50 mM, pH 7.5) containing 5 mM EDTA has proved best. Measurements are made on tissue samples with 0.67 mM G-6-P and 0.5 mM NADP, which are optimum concentrations for the enzyme from erythrocytes. G6P-DH is inhibited by primaquine and other 8-aminoquinolines (antimalarial drugs) in millimolar concentration, as well as by phenylhydrazine. Nevertheless, the therapeutic concentration of these substances is more than tenfold lower and therefore, they have no significant effect on the measurements.

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