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Effect of Alloxan Diabetes, Starvation and Refeeding on Glycolytic Kinase Activities in Rat Epididymal Adipose Tissue


THE levels of glucokinase, phosphofructokinase (PFK) and pyruvate kinase (PK) in the liver are decreased in alloxan diabetes and starvation, and are increased on refeeding1–3. Weber et al. have postulated that glycolysis may be, at least partially, controlled by the synchronous induction and repression of these regulatory enzymes through the action of hormones on a “functional genome”4. Changes of similar magnitude have not been observed in the heart with hexokinase (HK) (ref. 5) and PFK (ref. 6), but in epididymal fat pad, HK activity is markedly affected by these conditions7,8. The observed sensitivity of the PK in the fat pad to the allosteric effector fructose 1,6-diphosphate (Pogson, unpublished results), and the known kinetic properties of the PFK in the fat pad9, support the suggestion that these enzymes are of significance in the control of fat pad glycolysis. In view of these findings, it seemed important to determine whether the levels of all three kinases were responsive to conditions of alloxan diabetes, starvation and refeeding.

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POGSON, C., DENTON, R. Effect of Alloxan Diabetes, Starvation and Refeeding on Glycolytic Kinase Activities in Rat Epididymal Adipose Tissue. Nature 216, 156–157 (1967).

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