| Autor: |
Fujii, Shinya, Matsuda, Masafumi, Okuya, Shigeru, Yoshizaki, Yoshiki, Miura-Kora, Yukari, Kaneko, Toshio |
| Zdroj: |
Blood; October 1987, Vol. 70 Issue: 4 p1211-1213, 3p |
| Abstrakt: |
The hemolysate partially purified from human red cells was demonstrated to be capable of synthesizing fructose-2,6-bisphosphate (F-2,6-P2) from fructose-6-phosphate in the presence of adenosine triphosphate (ATP) indicating that human red cells contain fructose-6-phosphate,2-kinase. The effect of F-2,6-P2on the rate-limiting enzymes of glycolysis, ie, hexokinase, phosphofructokinase (PFK), and pyruvate kinase, has also been examined. PFK was activated by this metabolite and the half-maximum activation was obtained at a concentration of 10–7mol/L. Neither hexokinase nor pyruvate kinase was affected by F-2,6-P2. These results suggest that human erythrocytes may contain this metabolite as one of the positive effectors for PFK. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
