单克隆抗体AE-2可调节氨基甲酸酯类和有机磷酸酯类对胎牛血清乙酰胆碱酯酶的抑制作用。
Monoclonal antibody AE-2 modulates carbamate and organophosphate inhibition of fetal bovine serum acetylcholinesterase.
作者信息
Wolfe A D, Chiang P K, Doctor B P, Fryar N, Rhee J P, Saeed M
机构信息
Division of Biochemistry, Walter Reed Army Institute of Research, Washington, D.C. 20307-5100.
出版信息
Mol Pharmacol. 1993 Dec;44(6):1152-7.
The monoclonal antibody AE-2, raised against the human erythrocyte acetylcholinesterase (AChE) dimer (acetylcholine acetylhydrolase, EC 3.1.1.7), binds to other mammalian AChEs, including the tetramer that occurs in fetal bovine serum (FBS). AE-2 partially inhibited the rate of hydrolysis of the charged substrate acetylthiocholine by FBS AChE, whereas it increased the rate of hydrolysis of the neutral substrate indophenyl acetate. Present results show that AE-2 decreases the rate of inhibition of FBS AChE by the positively charged organophosphate amiton-p-toluene sulfonate and the positively charged carbamates pyridostigmine and neostigmine but accelerates inhibition of FBS AChE by the neutral organophosphates paraoxon and diisopropylfluorophosphate. Results suggest that AE-2 may allosterically modulate an anionic site in the catalytic center of FBS AChE.
针对人红细胞乙酰胆碱酯酶（AChE）二聚体（乙酰胆碱乙酰水解酶，EC 3.1.1.7）产生的单克隆抗体AE - 2，能与其他哺乳动物的AChE结合，包括胎牛血清（FBS）中的四聚体。AE - 2部分抑制了FBS AChE对带电荷底物乙酰硫代胆碱的水解速率，而它却提高了中性底物乙酸吲哚酚酯的水解速率。目前的结果表明，AE - 2降低了带正电荷的有机磷酸酯阿米妥 - 对甲苯磺酸盐以及带正电荷的氨基甲酸酯吡啶斯的明和新斯的明对FBS AChE的抑制速率，但加速了中性有机磷酸酯对氧磷和二异丙基氟磷酸对FBS AChE的抑制。结果表明，AE - 2可能通过变构调节FBS AChE催化中心的一个阴离子位点。
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