Journal of Clinical Investigation · 1961 · 121 citations · 49 references
Life SciencesBiochemistryPhysiologyBioenergeticsCellular MetabolismMetabolismCarbohydrate MetabolismEnergy MetabolismOxidative MetabolismPentose Phosphate PathwayPentose Phosphate Pathway RegulationTricarboxylic Acid CycleEnzymesGlucose-6-phosphate Dehydrogenase DeficiencyLactic Acid MetabolismPentose Phosphate Pathway DefectsPentose Phosphate Pathway FluxRed Blood Cell MetabolismTricarboxylic Acid Cycle FluxTricarboxylic Acid Cycle Metabolism
Mature human erythrocytes possess the enzymes necessary to catabolize glucose to CO2 via pentose phosphate pathway or to lactic acid via the Emb- den-Meyerhof pathway. These cells are deficient in certain enzymes of the tricarboxylic acid cycle. In the non-nucleated red cells, the oxidative reac- tions of pentose phosphate pathway appear to be the sole mechanism for glucose conversion to CO2 and for the generation of TPNH (2, 3). Several investigators have suggested that a major factor in the control of the rate of glucose catabo- lism via the pentose phosphate pathway is the meta- bolic demand for TPNH (4-6). It has been dem- onstrated that addition of dyes capable of acting as electron acceptors from TPNH (i.e., methylene blue, phenazine methosulphate, pyocyanin) in- creases the rate of activity of this pathway in eryth- rocytes, liver slices and mammary glands (7-9). Stimulation of the pentose phosphate pathway by pyruvate in bovine corneal epithelium, by insulin in rat mammary tissue, and by ammonium salts in yeasts has been ascribed to supply of substrates requiring TPNH for their metabolism or to stim- ulation of enzyme systems which utilize TPNH (8, 10-12).
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Lactic Dehydrogenase Activity in Blood.
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