Meisami E
J Neurochem. 1984 Mar;42(3):883-6. doi: 10.1111/j.1471-4159.1984.tb02766.x.
The study of Arrhenius plots for acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) activity from the rat brain and spinal cord revealed that in contrast to AChE, which exhibited biphasic Arrhenius plots with a distinct break (transition temperature) at about 16-18 degrees C, BuChE showed no evidence of discontinuity and a higher activation energy in the physiological range of temperature. The results indicate lack of lipid-protein interaction in the case of BuChE of the CNS tissue. It is inferred that BuChE, in contrast to AChE, is not bound in any significant way to cellular membranes of the CNS tissue.
对大鼠脑和脊髓中乙酰胆碱酯酶（AChE）和丁酰胆碱酯酶（BuChE）活性的阿伦尼乌斯曲线研究表明，与AChE在约16 - 18摄氏度时呈现出具有明显断点（转变温度）的双相阿伦尼乌斯曲线不同，BuChE在生理温度范围内没有不连续的迹象且活化能更高。结果表明中枢神经系统组织中的BuChE不存在脂 - 蛋白相互作用。据推测，与AChE不同，BuChE与中枢神经系统组织的细胞膜没有任何显著的结合方式。
