Abstract
The question of whether separate "membrane" and "soluble" pools of ATP exist in erythrocytes has been examined. Phosphoglycerate kinase (EC 2.7.2.3)-derived ("membrane") ATP was labeled by short-term incubation with inorganic [32P]phosphate. Pyruvate kinase (EC 2.7.1.40)-derived ("soluble")ATP is not labeled under these circumstances. The specific activity of the gamma-phosphate of "soluble" ATP was then evaluated by the addition of 2-deoxyglucose and measurement of the specific activity of 2-deoxyglucose-6-[32P]phosphate formed. This specific activity was essentially the same as the overall specific activity of erythrocyte ATP gama-phosphate, indicating that no functional pools of phosphoglycerate kinase-derived and pyruvate kinase-derived ATP exist in erythrocytes.
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Selected References
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