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- W75467315 abstract "Publisher SummaryThis chapter discusses inverse distribution of glycolytic and gluconeogenic enzymes in the liver lobule. The heterogeneity of hepatocytes is a phenomenon that has been established by morphological and histochemical studies. Recently, glucose-6-phosphatase was found to be located mainly periportally. This observation led to the assumption, that the pericentral hepatocytes may be enriched in glycolytic enzymes. To prove this hypothesis, phosphorenolpyruvate carboxykinase and pyruvate kinase, characteristic enzymes of the gluconeogenic and glycolytic pathways, were measured in single micro-dissected specimen from the periportal and pericentral areas of freeze-dried liver sections. Liver specimens from freeze dried tissue slices were obtained by the Lowry procedure. Enzyme activities were determined with microradiochemical (PEP-carboxykinase) and microfluorimetric (pyruvate kinase) procedures. Micro-dissection of freeze dried liver tissue resulted in cell groups of about 50 μm diameter, taken from the surrounding of the portal triad and the central vein respectively. In livers from fed rats, pyruvate kinase activity was about twice as high in the central as compared with the periportal cells of the liver lobule." @default.
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- W75467315 date "1977-01-01" @default.
- W75467315 modified "2023-09-27" @default.
- W75467315 title "INVERSE DISTRIBUTION OF GLYCOLYTIC AND GLUCONEOGENIC ENZYMES IN THE LIVER LOBULE" @default.
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- W75467315 doi "https://doi.org/10.1016/b978-0-12-691403-0.50041-0" @default.
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