The monoclonal antibody AE-2 modulates fetal bovine serum acetylcholinesterase substrate hydrolysis.
The monoclonal antibody (mAb) AE-2 decreases the rate of hydrolysis of acetylthiocholine (ATC) by fetal bovine serum acetylcholinesterase (acetylcholine acetylhydrolase EC 3.1.1.7) (FBS-AChE) (Doctor, B.P. et al. (1989) Proc. 32nd Oholo Conf., Eilat, Israel, in press), but increases the rate of hydrolysis (Vmax) of the nonpolar substrate, indophenyl acetate (IPA) approx. 15-fold. The affinity (Km) of FBS-AChE for IPA changes minimally in comparison with the increase in the rate of hydrolysis. The complex is dissociated, and the modulation of substrate hydrolysis is reversed by the active-center ligand, 1-methyl-2-hydroxyiminomethylpyridinium chloride (2-PAM).
Wolfe
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AD
Department of Applied Biochemistry, Walter Reed Army Institute of Research, Washington, DC 20307-5100.
D000110:Acetylcholinesterase / Q000097:blood* / Q000276:immunology; D000818:Animals; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D002417:Cattle; D007700:Kinetics; D013379:Substrate Specificity
D000911:Antibodies, Monoclonal; D000110:Acetylcholinesterase