Ogawa A, Nishi T, Furuya E, Watanabe F, Sakai A, Kido Y, Tsujinaka T, Mori T
Second Department of Surgery, Osaka University Medical School, Japan.
Biochem Mol Biol Int. 1993 May;30(1):83-90.
In order to investigate the effect of fructose on the metabolic rates of liver glycolysis, changes in fructose 2,6-bisphosphate content and fructose 6-phosphate, 2-kinase (F6P2kinase) activity were examined using perfused rat liver. When the starved liver was perfused with 0.5 mM fructose, the fructose 2,6-bisphosphate level was 6.66 nmol/g liver, or the maximum. However, with further increases in the fructose concentration, increments in the fructose 2,6-bisphosphate level gradually decreased. F6P2kinase was inactive in the starved rat liver. By perfusion with the medium containing fructose or even without fructose, however, the enzyme was activated. The suppression of the increase in the fructose 2,6-bisphosphate level by perfusion at higher fructose concentrations was at least partly due to the inhibition of F6P2kinase by F1P.
为了研究果糖对肝脏糖酵解代谢速率的影响,利用灌注大鼠肝脏检测了果糖-2,6-二磷酸含量以及果糖-6-磷酸-2-激酶(F6P2激酶)活性的变化。当饥饿的肝脏用0.5 mM果糖灌注时,果糖-2,6-二磷酸水平为6.66 nmol/g肝脏,即达到最大值。然而,随着果糖浓度进一步升高,果糖-2,6-二磷酸水平的增量逐渐减小。F6P2激酶在饥饿的大鼠肝脏中无活性。然而,通过用含果糖的培养基灌注甚至不用果糖灌注,该酶被激活。在较高果糖浓度下灌注对果糖-2,6-二磷酸水平升高的抑制至少部分是由于F1P对F6P2激酶的抑制。