马铃薯块茎中L(+)-乳酸脱氢酶的纯化及性质
Purification and properties of L(+)-lactate dehydrogenase from potato tubers.
作者信息
Davies D D, Davies S
出版信息
Biochem J. 1972 Oct;129(4):831-9. doi: 10.1042/bj1290831.
Abstract
- A purification of l(+)-lactate dehydrogenase is described. 2. The final preparation is active with NADH and NADPH and with a number of keto acids, but evidence is presented to support the view that a single enzyme is involved. 3. NAD(+) showed product inhibition, but at slightly acid pH values there was evidence of co-operative binding. 4. At acid pH values ATP was a potent inhibitor and appears to be an allosteric effector. At neutral or alkaline pH values ATP behaved as a weak competitive inhibitor. 5. The physiological significance of inhibition by ATP is discussed.
摘要
- 描述了l(+)-乳酸脱氢酶的一种纯化方法。2. 最终制剂对NADH和NADPH以及多种酮酸具有活性，但有证据支持涉及单一酶的观点。3. NAD(+)表现出产物抑制作用，但在略酸性pH值下有协同结合的证据。4. 在酸性pH值下，ATP是一种强效抑制剂，似乎是一种别构效应剂。在中性或碱性pH值下，ATP表现为弱竞争性抑制剂。5. 讨论了ATP抑制作用的生理意义。
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