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- W2047303514 abstract "Abstract. Assay of seven glycolytic enzymes, steady-state levels of glycolytic metabolites, oxidized and reduced glutathione, inorganic phosphate, adenine nucleotides, sodium and potassium, and various incubation experiments were performed on red cells isolated from children with Duchenne-Erb muscular dystrophy. The activity of hexokinase, aldolase, pyruvate kinase, and the levels of glucose-6-phosphate, ADP and intracellular inorganic phosphate were significantly increased. Long term incubation (15 h at 4° C) showed a phosphofructokinase activation; during shorter incubation (3 h at pH 7.6 and 38° C) similar behaviour of glycolytic metabolites, 2,3-diphosphoglycerate and adenine nucleotides was observed in both normal and dystrophic red cells, while the lactate output was greater in the latter. The regulation of phosphoglycerate kinase and pyruvate kinase in vivo followed a normal pattern. Addition of ouabain to red cells incubated in a low-potassium buffer was followed by increase of ATP in the normal and a decrease in the dystrophic red cell. Ouabain had no effect on glycolytic metabolites in the dystrophic cell, whereas sharp increases of fructose-1,6-diphosphate and dihydroxyacetone-phosphate were observed in the normal cell." @default.
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- W2047303514 date "1971-12-01" @default.
- W2047303514 modified "2023-09-28" @default.
- W2047303514 title "Red Cell Glycolysis in the Myo dystrophic Child" @default.
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- W2047303514 doi "https://doi.org/10.1111/j.1365-2362.1971.tb00551.x" @default.
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