钠泵三磷酸腺苷酶的磷脂酰丝氨酸激活作用的温度依赖性
The temperature dependence of activation by phosphatidylserine of the sodium pump adenosine triphosphatase.
作者信息
Priestland R N, Whittam R
出版信息
J Physiol. 1972 Jan;220(2):353-61. doi: 10.1113/jphysiol.1972.sp009711.
Abstract
- Treatment of rabbit brain homogenates with deoxycholate reduced ouabain-insensitive ATPase sixfold and subsequently adding phosphatidylserine had no effect. Ouabain-sensitive ATPase was made entirely latent but it was fully restored on adding phosphatidylserine.2. Temperature and pH were varied to see if the reconstituted system resembled that in the original membranes. Linear Arrhenius plots were always obtained with the homogenate, and the activation energy was higher for the ouabain-sensitive than for the ouabain-resistant enzyme.3. A break at about 15 degrees C was found in the Arrhenius plot of the reconstituted enzyme, but there was no break without added phosphatidylserine or when ouabain was added. The break suggests that the conformation and catalytic activity of the enzyme protein depended on the physical state of phosphatidylserine.
摘要
- 用脱氧胆酸盐处理兔脑匀浆可使哇巴因不敏感的ATP酶活性降低六倍，随后添加磷脂酰丝氨酸则无作用。哇巴因敏感的ATP酶完全变为潜伏状态，但添加磷脂酰丝氨酸后可完全恢复。2. 改变温度和pH值以观察重构系统是否与原始膜中的系统相似。匀浆始终得到线性阿伦尼乌斯图，且哇巴因敏感酶的活化能高于哇巴因抗性酶。3. 在重构酶的阿伦尼乌斯图中发现约15℃处有一个断点，但在未添加磷脂酰丝氨酸或添加哇巴因时没有断点。该断点表明酶蛋白的构象和催化活性取决于磷脂酰丝氨酸的物理状态。
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