Abstract
Human platelets contain fructose 2,6-bisphosphate, 6-phosphofructo-l-kinase (ATP: D-Fructose-6-phosphate-1-phosphotransferase, E.C.2.7. 1.11), the rate-limiting enzyme in platelet glycolysis appear to be significantly activated by physiological concentration of the compound, suggesting for fructose 2,6-bisphosphate a key regulatory role in the control of the glycolytic flux. Incubation of human platelets with thrombin results in a parallel and rapid increase of fructose-2,6-bisphosphate levels and glycolytic flux, suggesting that the compound may also be involved in the enhancement of glycolysis elicited by the stimulating agent.
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