Klinar B, Kamarić L, Sketelj J, Brzin M
Neurochem Res. 1985 Jun;10(6):797-808. doi: 10.1007/BF00964537.
Amphiphile dependency, solubility in aqueous solutions, and sensitivity to proteolysis of acetylcholinesterase (AChE) and nonspecific cholinesterase (nsChE) in the rat superior cervical ganglion were studied and compared to properties of soluble plasma cholinesterases. Ganglion AChE shows strong amphiphile dependency: an amphyphilic substance must be present in the homogenizing medium in order to obtain maximal apparent enzyme activity. Apparent activity of AChE solubilized in Ringer's solution was also increased after subsequent addition of a detergent. The 4 S molecular form, predominant in this extract (corresponding to the fastest electrophoretic band), is very sensitive to papain proteolysis but can be protected by a detergent. This molecular form therefore carries an important hydrophobic domain and is probably membrane bound in situ. The 10 S form of ganglionic AChE, extracted in Ringer's solution, is probably a soluble enzyme since, like soluble plasma enzymes, it is not amphiphile dependent and is rather resistant to proteolysis. Ganglion nsChE is more water soluble, less amphiphile dependent and more protease resistant than AChE.
研究了大鼠颈上神经节中乙酰胆碱酯酶（AChE）和非特异性胆碱酯酶（nsChE）的两亲性依赖性、在水溶液中的溶解度以及对蛋白水解的敏感性，并与可溶性血浆胆碱酯酶的特性进行了比较。神经节AChE表现出很强的两亲性依赖性：为了获得最大的表观酶活性，在匀浆介质中必须存在一种两亲性物质。在林格氏溶液中溶解的AChE的表观活性在随后添加去污剂后也有所增加。在该提取物中占主导地位的4S分子形式（对应于最快的电泳带）对木瓜蛋白酶水解非常敏感，但可以被去污剂保护。因此，这种分子形式带有一个重要的疏水结构域，可能在原位与膜结合。在林格氏溶液中提取的神经节AChE的10S形式可能是一种可溶性酶，因为与可溶性血浆酶一样，它不依赖两亲性，并且对蛋白水解具有相当的抗性。神经节nsChE比AChE更易溶于水，对两亲性的依赖性更小，对蛋白酶的抗性更强。
