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谷氨酸脱氢酶系统的平衡常数。

The equilibrium constants of the glutamate dehydrogenase systems.

作者信息

Engel P C, Dalziel K

出版信息

Biochem J. 1967 Nov;105(2):691-5. doi: 10.1042/bj1050691.

Abstract
  1. Equilibrium constants for the oxidation of glutamate by NAD(+) and NADP(+), catalysed by glutamate dehydrogenase, have been measured in phosphate buffers of different ionic strengths and at several temperatures. 2. The equilibrium constants for both systems vary markedly with ionic strength. Thermodynamic values for the two systems obtained by extrapolation to zero ionic strength differ significantly from one another. The standard free-energy change for NADP(+) reduction has been calculated from that for NAD(+) reduction. 3. The heat of reaction has been estimated and is the same with both coenzymes. 4. The thermodynamic data are discussed in relation to earlier data.
摘要
  1. 已在不同离子强度的磷酸盐缓冲液中以及几个温度下测定了由谷氨酸脱氢酶催化的NAD(+)和NADP(+)氧化谷氨酸的平衡常数。2. 两个系统的平衡常数均随离子强度显著变化。通过外推至零离子强度获得的两个系统的热力学值彼此有显著差异。已根据NAD(+)还原的标准自由能变化计算出NADP(+)还原的标准自由能变化。3. 已估算出反应热,两种辅酶的反应热相同。4. 结合早期数据对热力学数据进行了讨论。

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