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CONTROL OF AEROBIC GLYCOLYSIS AND PYRUVATE KINASE ACTIVITY IN CEREBRAL CORTEX SLICES
Author(s) -
Takagaki G.
Publication year - 1968
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1968.tb11632.x
Subject(s) - glycolysis , pyruvate kinase , phosphofructokinase , hexokinase , anaerobic glycolysis , glyceraldehyde , biochemistry , pyruvate dehydrogenase complex , cerebral cortex , glyceraldehyde 3 phosphate dehydrogenase , calcium , chemistry , biology , endocrinology , dehydrogenase , metabolism , enzyme , organic chemistry
— —The concentrations of glycolytic intermediates were measured in aerobically incubated guinea pig cerebral cortex slices. Increasing the concentration of potassium in the medium increased fructose diphosphate ten‐fold and triose phosphates three‐fold. Omitting calcium increased all the glycolytic intermediates except pyruvate; triose phosphates were increased most. The changed patterns of the glycolytic intermediate profile in the slices are consistent with the previously proposed hypothesis that the phosphofructokinase is a main regulatory step in glycolysis. Glycolysis is also limited at the step of pyruvate kinase, which is inhibited in cerebral cortex slices. Calcium in the tissue and cellular organization of the slices were shown to be responsible for this inhibition. It was concluded that the effects of potassium and calcium on aerobic glycolysis in cerebral cortex slices are direct—on the pyruvate kinase—and also indirect. Calcium was shown to be inhibitive also to the activities of hexokinase, phosphoglucoisomerase, phosphofructokinase, glyceraldehyde 3‐phosphate dehydrogenase and enolase of guinea pig cerebral tissue.