Monoclonal antibody AE-2 modulates carbamate and organophosphate inhibition of fetal bovine serum acetylcholinesterase. (Reannouncement with new availability information)
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). AE2 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 amition-p-toluene sulfonate and the positively charged carbamates pyridostigmine and neostigmine but accelerate inhibition of FBS AChE by neutral organophosphates paraoxon and diisopropylfluorophosphate. Results suggest that AE-2 may allosterically modulate an anionic site in the catalytic center of FBS AChE.
- Research Organization:
- Walter Reed Army Inst. of Research, Washington, DC (United States). Div. of Biochemistry
- OSTI ID:
- 210769
- Report Number(s):
- AD-A-279000/4/XAB; WR-048-94; TRN: 60640368
- Resource Relation:
- Other Information: PBD: 1993
- Country of Publication:
- United States
- Language:
- English
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