Fructose 2,6-bisphosphate in relation with the resumption of metabolic activity in slices of Jerusalem artichoke tubers

When slices of Jerusalem artichoke tubers were incubated at 25°C, their concentration in fructose 2,6-bisphosphate increased up to 250-fold within 2 h. Fructose 2,6-bisphosphate was also formed, although at a slower rate, in slices incubated at 0°C. Its formation could not be explained by an increase in the concentration of fructose 6-phosphate or of ATP either by an activation of phosphofructo-2-kinase. Pyrophosphate—fructose-6-phosphate 1-phosphotransferase was the only enzyme present in a tuber extract which was found to be sensitive to fructose 2,6-bisphosphate. An improved procedure for the assay of fructose 2,6-bisphosphate is also reported.