Abstract
Summary
In a preparation of cultured cells (human KB) concentrations of ATP and of fructose-1,6-diphosphate are markedly sensitive to change in external pH. In a series of experiments when the pH was increased from 7.0 to 8.0, the average value for the content of ATP decreased from 9.1 to 1.0 μmole/g of protein while that for fructose-1,6-diphosphate increased from 1.5 to 16.1 μ, mole/g of protein. The changes reverse when the pH is returned to 7.0. The reaction is linked to inhibition rather than stimulation of the rate of glycolysis, and the effect can be simulated by adding iodoace-tate without changing pH. The inverse relationship between ATP and FDP after changing pH has also been observed in Ehr-lich ascites tumor cells.
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