Affiliation:
1. Department of Biochemistry, Faculty of Medicine, University of Sevilla, Spain.
Abstract
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.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
12 articles.
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1. The Erythrocyte;Clinical Biochemistry of Domestic Animals;2008
2. The Erythrocyte;Clinical Biochemistry of Domestic Animals;1997
3. Characterization of phosphofructokinase-deficient canine erythrocytes;Journal of Inherited Metabolic Disease;1992-09
4. Activating effect of adenosine on rat erythrocyte glycolysis;International Journal of Biochemistry;1992-03
5. A stimulatory effect of FFA on glycolysis unmasked in cells with impaired oxidative capacity.;American Journal of Physiology-Endocrinology and Metabolism;1990-09