大鼠肝脏葡萄糖激酶的动力学。在生理相关浓度下与葡萄糖的协同相互作用。
Kinetics of rat liver glucokinase. Co-operative interactions with glucose at physiologically significant concentrations.
作者信息
Storer A C, Cornish-Bowden A
出版信息
Biochem J. 1976 Oct 1;159(1):7-14. doi: 10.1042/bj1590007.
Abstract
The kinetics of glucokinase from rat liver were studied over wide ranges of glucose and MgATP2- concentrations. The initial rate shows a co-operative dependence on the glucose concentration, with Hill coefficients in the range 1.2-1.5. The degree of glucose co-operativity increases with the MgATP2- concentration, but no co-operativity was detected for the dependence of the rate on the MgATP2- concentration. The effects observed occur at physiologically reasonable concentrations of glucose and MgATP2- and are consistent with the presumed function of glucokinase in maintaining a constant concentration of glucose in the blood.
摘要
在很宽的葡萄糖和MgATP2-浓度范围内研究了大鼠肝脏葡萄糖激酶的动力学。初始速率显示出对葡萄糖浓度的协同依赖性，希尔系数在1.2 - 1.5范围内。葡萄糖协同作用的程度随MgATP2-浓度增加而增加，但未检测到速率对MgATP2-浓度依赖性的协同作用。观察到的效应发生在葡萄糖和MgATP2-的生理合理浓度下，并且与葡萄糖激酶在维持血液中葡萄糖浓度恒定方面的假定功能一致。
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