Cabezas-Herrera J, Campoy F J, Vidal C J
Departamento de Bioquímica y Biología Molecular, Universidad de Murcia, Spain.
Neurochem Res. 1992 Jul;17(7):717-22. doi: 10.1007/BF00968011.
The action of ethanol on the activity of membrane-bound and soluble acetylcholinesterase (AChE) in sarcoplasmic reticulum of skeletal muscle has been studied. Treatment of membranes with 2.5-12.5% v/v ethanol produced a slight stimulation of the AChE activity and inhibition at higher concentration. The enzyme remained associated with the membranes after these treatments. The enzyme solubilized with Triton X-100 was inhibited by ethanol in a time-independent manner. Isolated 16 S (A12), 10.5 S (G4) and 4.5 S (G1) forms of AChE were inhibited by ethanol to a similar extent. Samples were reversibly inhibited by ethanol, up to 12.5% v/v, and irreversibly at higher concentrations. Kinetic studies performed with isolated forms in the presence of 5-12.5% v/v ethanol showed that the solvent behaved as a competitive inhibitor of the asymmetric form but as a mixed inhibitor of the tetrameric and monomeric forms. The results show that the solvent interacts with active and/or regulatory sites of AChE from muscle microsomes.
已对乙醇对骨骼肌肌浆网中膜结合型和可溶性乙酰胆碱酯酶（AChE）活性的作用进行了研究。用2.5 - 12.5%（v/v）乙醇处理膜会使AChE活性略有刺激，而在较高浓度下则产生抑制作用。这些处理后酶仍与膜结合。用Triton X - 100增溶的酶被乙醇以与时间无关的方式抑制。分离出的16 S（A12）、10.5 S（G4）和4.5 S（G1）形式的AChE被乙醇抑制的程度相似。样品在高达12.5%（v/v）的乙醇浓度下被可逆抑制，在更高浓度下则被不可逆抑制。在存在5 - 12.5%（v/v）乙醇的情况下对分离形式进行的动力学研究表明，该溶剂对不对称形式表现为竞争性抑制剂，而对四聚体和单体形式表现为混合型抑制剂。结果表明，该溶剂与肌肉微粒体中的AChE活性和/或调节位点相互作用。
