Abstract
Synthetase D phosphatase activity in a liver glycogen pellet preparation is inhibited by ATP (physiological concentration). The inhibition can be reversed by glucose concentrations within the usual physiological range. Phosphophosphorylase activity decreases concomitantly with increasing synthetase I activity during the phosphatase incubation but the decrease is modest even in the presence of glucose. The glucose reversal of ATP inhibition is not the result of ATPase or glucokinase activities, which would reduce the ATP concentration. ATP, glucose and glucose 6-phosphate concentrations remain stable during the phosphatase assay.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 164-171 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 53 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jul 2 1973 |