低压环境下大鼠肝脏琥珀酸脱氢酶的激活
Activation of liver succinate dehydrogenase in rats exposed to hypobaric conditions.
作者信息
Aithal H N, Ramasarma T
出版信息
Biochem J. 1969 Oct;115(1):77-83. doi: 10.1042/bj1150077.
Abstract
- On brief exposure of rats to hypobaric conditions, the activity of hepatic mitochondrial succinate dehydrogenase was raised from the basal state to a ;partially activated state'. This was further raised to ;fully activated state' by preincubation of mitochondria with succinate, as was the activity in mitochondria from normal rats. 2. On washing mitochondria with the homogenizing sucrose medium the activity excess obtained on preincubation with succinate was lost in mitochondria from both normal and treated rats. 3. The enzyme in the ;partially activated state' from animals exposed to hypobaric conditions was stable to the washing procedure but was labilized and reverted to a low basal state of activity on freezing and thawing of the isolated mitochondria. 4. The results suggest that activation of succinate dehydrogenase under hypobaric conditions represents a conformational change leading to a stable, partially activated, form of the enzyme system: this is the first evidence of physiological modulation of this rate-limiting step in the control of the rate of oxidation of succinate.
摘要
- 将大鼠短暂暴露于低压环境中，肝脏线粒体琥珀酸脱氢酶的活性从基础状态提高到“部分激活状态”。通过用琥珀酸预孵育线粒体，其活性进一步提高到“完全激活状态”，正常大鼠线粒体中的活性也是如此。2. 用匀浆蔗糖培养基洗涤线粒体后，正常大鼠和处理大鼠的线粒体中，用琥珀酸预孵育后获得的活性过量部分均丧失。3. 暴露于低压环境的动物处于“部分激活状态”的酶对洗涤过程稳定，但在分离的线粒体冻融后会变得不稳定，并恢复到低基础活性状态。4. 结果表明，低压条件下琥珀酸脱氢酶的激活代表一种构象变化，导致酶系统形成稳定的部分激活形式：这是控制琥珀酸氧化速率这一限速步骤的生理调节的首个证据。
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