2-Deoxy-d-galactose Metabolism in Ascites Hepatoma Cells Results in Phosphate Trapping and Glycolysis Inhibition
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چکیده
منابع مشابه
Inhibition of anaerobic glycolysis in Ehrlich ascites tumor cells by 2-deoxy-D-glucose.
Little is known of the mechanisms by which 2-deoxy-D-glucose (2-DG) inhibits anaerobic glycolysis in yeast cells (1, 9, 13, 14) and in brain, diaphragm, and liver slices (15). This compound also inhibits anaerobic glycolysis in various tumors (15), prolongs the survival time of mice bearing the Krebs ascites carcinoma (2), and causes a decreased rate of growth of several tumors in rats or mice ...
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Little is known of the mechanisms by which %deoxy-n-glucose (a-DG) inhibits anaerobic glycolysis in yeast cells (1, 9, 18, 14) and in brain, diaphragm, and liver slices (15). This compound also inhibits anaerobic glycolysis in various tumors (15), prolongs the survival time of mice bearing the Krebs ascites carcinoma (a), and causes a decreased rate of growth of several tumors in rats or mice (...
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UNLABELLED Accurate quantification of regional liver function is needed, and PET of specific hepatic metabolic pathways offers a unique method for this purpose. Here, we quantify hepatic galactose elimination in humans using PET and the galactose analog 2-(18)F-fluoro-2-deoxy-d-galactose ((18)F-FDGal) as the PET tracer. METHODS Eight healthy human subjects underwent (18)F-FDGal PET/CT of the ...
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A study of the enzymes of the glycogen pathway in Novikoff ascites hepatoma shows that glycogen synthetase has the lowest activity and that the tumour contains no high-K(m) soluble glucokinase. However, incubation of tumour cells with metabolizable sugars in vitro, or intraperitoneal administration of glucose into the tumour-bearing rat, results in glycogen accumulation by the tumour cells. Gly...
متن کاملLactose and D-galactose metabolism in Staphylococcus aureus. II. Isomerization of D-galactose 6-phosphate to D-tagatose 6-phosphate by a specific D-galactose-6-phosphate isomerase.
The inducible D-galactose-6-phosphate isomerase that functions in the metabolism of lactose and D-galactose in Staphylococcus aureus was partially purified from extracts of D-galactose-grown cells. It was shown to catalyze specifically the reversible isomerization of D-galactose 6-phosphate to D-tagatose 6-phosphate, the apparent Km values being 9.6 mM and 1.9 mM, respectively. At equilibrium, ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1977
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1977.tb11293.x