Sobrino, F.
Rider, Mark H.
[UCL]
Gualberto, A
Hue, Louis
[UCL]
The concentration of fructose 2,6-bisphosphate found in freshly isolated erythrocytes was below the limit of detection (20 pmol/ml of packed cells). However, it increased to about 250 pmol/ml of cells when erythrocytes were incubated with glucose at pH 6.9, but not at pH 7.4 or 8.2. This could be explained by variations in the content of glycerate 2,3-bisphosphate, which was found to inhibit 6-phosphofructo-2-kinase, the enzyme responsible for fructose 2,6-bisphosphate synthesis. Glycerate 2,3-bisphosphate was also found to inhibit the potato enzyme (pyrophosphate:fructose-6-phosphate 1-phosphotransferase) used for the measurement of fructose 2,6-bisphosphate.
Bibliographic reference |
Sobrino, F. ; Rider, Mark H. ; Gualberto, A ; Hue, Louis. Fructose 2,6-bisphosphate in rat erythrocytes. Inhibition of fructose 2,6-bisphosphate synthesis and measurement by glycerate 2,3-bisphosphate.. In: The Biochemical journal, Vol. 244, no. 1, p. 235-8 (1987) |
Permanent URL |
http://hdl.handle.net/2078.1/25937 |