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目的比较氨基甲酸酯与有机磷酸酯抑制乙酰胆碱酯酶（ＡＣｈＥ）活力的毒性机制。方法以小鼠红细胞ＡＣｈＥ为酶源，吡啶斯的明、毒扁豆碱与沙林为酶抑制剂，２ＰＡＭ·Ｃｌ为中毒酶重活化剂，改进的微量ＤＴＮＢ法测定酶活力。通过交叉抑制实验，比较中毒酶的重活化率。结果吡啶斯的明与沙林交叉抑制后中毒酶的重活化率（８．０％与１０．５％，４５．１％与４７．３％）比较、毒扁豆碱与沙林交叉抑制后中毒酶的重活化率（－７．０％与－９．９％，４０．６％与４６．７％）比较，均未具明显差异。结论推测氨基甲酸酯与有机磷酸酯抑制ＡＣｈＥ作用于同一部位，即酶活性中心的丝氨酸羟基上
Objective To compare the toxicity mechanism of carbamate and organophosphate in inhibiting the activity of acetylcholinesterase (AChE). Methods The mouse erythrocyte AChE enzyme source, pyridostigmine, physostigmine and sarin as enzyme inhibitors, 2 PAMAM as a toxin activator, modified DTNB method to measure the enzyme activity. Cross-inhibition experiments were performed to compare the rate of reactivation of the toxic enzymes. Results The rates of reactivation (8.0% vs. 10.5%, 45.1% vs. 47.3%) of the inactivated phytase after cross-inhibition of pyridostigmine and sarin were significantly lower than those of sarin Enzyme reactivation rates (-7.0% vs. -9.9%, 40.6% vs. 46.7%) did not differ significantly. Conclusion It is speculated that carbamate and organic phosphate inhibit the action of AChE on the same site, that is, the serine hydroxy group at the active site