Begum S J, Reddy M M, Indira K, Swami K S
Department of Zoology, S. V. University, Tirupati, India.
Arch Int Physiol Biochim. 1987 Jun;95(2):101-4. doi: 10.3109/13813458709104521.
Substrate kinetics of acetylcholinesterase (AChE) were investigated in control and dieldrin-treated Mus booduga brains. Non competitive inhibition with respect to activation by acetylcholine was indicated by decreased maximal velocity (V) without change in Michaelis-Menten constant (Km). Activation energies (delta E) were found to be increased suggesting decreased efficiency of enzyme in dieldrin-treated mouse brains. Fall in the activity potential of AChE may account for the interference of dieldrin or its metabolites with the acetylcholine (ACh)--AChE system and deserve consideration in contributing to the neurotoxicity.
在对照和经狄氏剂处理的印度姬鼠大脑中研究了乙酰胆碱酯酶（AChE）的底物动力学。最大速度（V）降低而米氏常数（Km）不变，表明对乙酰胆碱激活存在非竞争性抑制。发现活化能（δE）增加，提示在经狄氏剂处理的小鼠大脑中酶的效率降低。AChE活性电位的下降可能解释了狄氏剂或其代谢产物对乙酰胆碱（ACh）-AChE系统的干扰，并且在导致神经毒性方面值得考虑。
