Accession Number : ADP008811
Title : Modulation of Acetylcholinesterase by Monoclonal Antibody AE-2.
Corporate Author : WALTER REED ARMY INST OF RESEARCH WASHINGTON DC
Personal Author(s) : Wolfe, A. D. ; Chiang, P. K. ; Doctor, B. P. ; Rhee, J. P. ; Saeed, M.
Report Date : 13 MAY 1993
Pagination or Media Count : 9
Abstract : The monoclonal antibody AE-2 was raised against the human erythrocyte dimer acetylcholinesterase (AChE; acetylcholine acetyl-hydrolase, EC 184.108.40.206), but bound to other mammalian AChEs, including the tetramer which occurs in fetal bovine serum (FBS). AE-2 partially inhibited the rate of hydrolysis of the charged substrate acetylthiocholine (ATC) by FBS AChE, while it increased the rate of hydrolysis of the neutral substrate, indophenyl acetate (IPA). Present results show AE-2 to decrease the rate of inhibition of FBS AChE by the positively charged organophosphate (OP), amiton-p-toluene sulfonate, and the positively charged carbamates (CB) pyridostigmine and neostigmine, but, consistent with its effects upon ATC and IPA, to accelerate inhibition of FBS AChE by the neutral OPs, paraoxon and diisopropylfluorophosphate (DFP). Results suggest that AE-2 may allosterically modulate an anionic site facilitating access to the catalytic center of FBS AChE.
Descriptors : *ACETYLCHOLINESTERASE, *MONOCLONAL ANTIBODIES, *ERYTHROCYTES, ACETATES, ACETYLCHOLINE, ANTIBODIES, BOVINES, CARBAMATES, DIMERS, HUMANS, HYDROLASES, HYDROLYSIS, INHIBITION, NEUTRAL, ORGANOPHOSPHATES, PARASYMPATHOMIMETIC AGENTS, SITES, SUBSTRATES, SULFONATES, TOLUENES, PHARMACOKINETICS.
Subject Categories : Biochemistry
Distribution Statement : APPROVED FOR PUBLIC RELEASE