Partial purification of a rat liver enzyme that catalyzes the formation of fructose 2,6-bisphosphate.
Partial purification of a rat liver enzyme that catalyzes the formation of fructose 2,6-bisphosphate.
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部分纯化催化果糖 2,6-二磷酸形成的大鼠肝酶。
DOI：
10.1016/0006-291x(81)91858-1
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发表时间：
1981
影响因子：
3.1
通讯作者：
Pilkis,SJ
中科院分区：
文献类型：
--
作者：
El-Maghrabi,MR;Claus,TH;Pilkis,J;Pilkis,SJ
在大鼠肝胞液中检测到6-磷酸果糖2-激酶（ATP：D-果糖-6-磷酸2-磷酸转移酶）活性。经硫酸铵分级沉淀、DEAE-Cellulose柱层析和Sephadex G-100凝胶过滤等方法对酶进行了部分纯化。该酶催化磷酸从ATP转移到6-磷酸果糖的C2位。6-磷酸果糖的Km值为0.5mM，ATP的Km值为0.2mM，表明2，6-二磷酸果糖是通过这种独特的酶反应合成的。
A 6-phosphofructo 2-kinase (ATP:D-fructose-6-phosphate 2-phosphotransferase) activity was detected in rat liver cytosol. The enzyme was partially purified by (NH4)2SO4fractionation, DEAE-Cellulose chromatography, and gel filtration on Sephadex G-100. This enzyme catalyzed the transfer of phosphate from ATP to the C2 position of fructose 6-phosphate. The apparent Kmfor fructose 6-phosphate was 0.5 mM while that for ATP was 0.2 mM. It is suggested that fructose 2,6-bisphosphate is synthesized via this unique enzyme reaction.