Burgun C, Warter J M, Veil P, Cremel G, Waksman A
Biochimie. 1980;62(10):671-80. doi: 10.1016/s0300-9084(80)80024-1.
Acetylcholinesterase (Acetylcholine acetylhydrolase E.C. 3.1.1.7.) released from a rat brain synaptosomal fraction was shown to rebind upon incubation in the presence of 3 mM acetylcholine. This action was shown to be reversible. Glutamate, aspartate and gamma-aminobutyrate antagonise this effect. Solubilization of both bulk protein and acetylcholinesterase by Lubrol WX and triton X 100 after acetylcholine incubation of synaptosomal fractions is much lower than in the non incubated preparation. Local production of protons due to the hydrolysis of acetylcholine by the enzyme could partially explain the reassociation of the enzyme. We suggest that the observed phenomenon may play some physiological role in the function of acetylcholinesterase.
从大鼠脑突触体组分释放的乙酰胆碱酯酶（乙酰胆碱乙酰水解酶，E.C. 3.1.1.7.）在3 mM乙酰胆碱存在下孵育时会重新结合。该作用被证明是可逆的。谷氨酸、天冬氨酸和γ-氨基丁酸可拮抗这种作用。突触体组分在乙酰胆碱孵育后，经Lubrol WX和曲拉通X 100溶解的总蛋白和乙酰胆碱酯酶比未孵育的制剂低得多。酶水解乙酰胆碱导致的质子局部产生可能部分解释了酶的重新结合。我们认为观察到的现象可能在乙酰胆碱酯酶的功能中发挥一些生理作用。
