磷酸化对大鼠肝脏果糖-1,6-二磷酸酶动力学性质的影响。
Effects of phosphorylation on the kinetic properties of rat liver fructose-1,6-bisphosphatase.
作者信息
Meek D W, Nimmo H G
出版信息
Biochem J. 1984 Aug 15;222(1):125-30. doi: 10.1042/bj2220125.
Abstract
A new purification procedure for rat liver fructose-1,6-bisphosphatase that involves use of Procion Red-Sepharose is described. The purified enzyme was homogeneous, had a subunit Mr of 40 000-41 000 and seemed to be undegraded. The enzyme could be phosphorylated by cyclic AMP-dependent protein kinase with a stoicheiometry of one per subunit. Phosphorylation caused a 2-fold decrease in the Km of the enzyme for fructose 1,6-bisphosphate, but did not affect its allosteric responses to AMP, Mg2+ and fructose 2,6-bisphosphate.
摘要
本文描述了一种新的大鼠肝脏果糖-1,6-二磷酸酶纯化方法，该方法涉及使用Procion Red-Sepharose。纯化后的酶是均一的，亚基分子量为40000 - 41000，且似乎未被降解。该酶可被环磷酸腺苷依赖性蛋白激酶磷酸化，每个亚基的化学计量比为1。磷酸化使该酶对果糖1,6-二磷酸的米氏常数降低了2倍，但不影响其对AMP、Mg2+和果糖2,6-二磷酸的变构反应。
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