Brimijoin S, Carter J
J Neurochem. 1982 Feb;38(2):588-90. doi: 10.1111/j.1471-4159.1982.tb08667.x.
The turnover of acetylcholinesterase (AChE) and its molecular forms was measured by following the loss of enzyme activity in the right hemidiaphragms of Sprague-Dawley rats treated with cycloheximide, 20 mg/kg, every 4 h. This treatment inhibited 96% of the incorporation of [3H]leucine into muscle protein. After 8 h of treatment, the total AChE activity of the diaphragm decreased by 17% (P less than 0.01). Assuming first-order exponential kinetics, a half-life of 30 h and an hourly turnover of 180 units were calculated. The measured accumulation of AChE activity at a ligature on the phrenic nerve indicated that axonal transport contributed trivially to this turnover. Sucrose density gradient experiments showed that the cycloheximide-induced low of AChE activity was restricted to the 4S enzyme, which had an apparent half-life of 6.2 h.
通过追踪用环己酰亚胺（20mg/kg，每4小时一次）处理的Sprague-Dawley大鼠右半膈肌中酶活性的丧失来测定乙酰胆碱酯酶（AChE）的周转率及其分子形式。这种处理抑制了96%的[3H]亮氨酸掺入肌肉蛋白。处理8小时后，膈肌的总AChE活性下降了17%（P<0.01）。假设为一级指数动力学，计算出半衰期为30小时，每小时周转率为180单位。在膈神经结扎处测得的AChE活性积累表明轴突运输对这种周转率的贡献微不足道。蔗糖密度梯度实验表明，环己酰亚胺诱导的AChE活性降低仅限于4S酶，其表观半衰期为6.2小时。
