Distinction between Acetylcholine-Esterase and Other Choline Ester-splitting Enzymes

Two selective inhibitors of cholinesterase

“…test is available. Augustinsson (1948) has argued that the optimum substrate concentration ought to be increased in the presence of a competitive inhibitor, and has produced some evidence in support (see also Augustinsson & Nachmansohn, 1949 (Fig. 2).…”

The Action of Carbamic Esters and Tetraethylpyrophosphate on Normal and Curarized Frog Rectus Muscle

“…Table I) that these differences in sensitizing capacity are not due to differences in cholinesterase inhibition. It must further be emphasized that with TEPP a rapid irreversible combination with cholinesterase occurs (Augustinsson and Nachmansohn, 1949). However, with the carbamic esters, which combine reversibly with cholinesterase, the figures for cholinesterase inhibition in our experiments with 90 seconds' exposure to Ach or other drugs are higher than those summarized in Table I, since sufficient time is not allowed for the establishment of an equilibrium between the reacting components cholinesterase, Ach and inhibitor (Goldstein, 1944;Goldstein et al, 1949).…”

Recovery of Acetylcholinesterase Activity in the Common Carp ( Cyprinus carpio L.) After Inhibition by Organophosphate and Carbamate Compounds

“…The acetylcholinesterase or "true cholinesterase" (AChE EC.3.1.1.8) predominantly associated with nervous tissue and erythrocytes, and the pseudo cholinesterase (ChE EC: 3.1.1.7) which is found in the serum, muscle and ganglia (Fossi et al 1995;Harel et al 1992;Vigny et al 1978). These two enzymes, AChE and ChE can be distinguished not only by their distribution but also by their substrate specificity and their sensitivity to certain selective inhibitors (Augustisson and Nachmanshon 1949;Davison 1955;Toutant et al 1985;Vigny et al 1978). Both AChE and ChE are inhibited by eserine but only AChE is inhibited by 1.5-bis(4-allyl dimethyl amino phenyl)pentan-3-one dibromide (BW284C51) and by an excess of substrate, for example acetylthiocholine chloride (ACh) (Augustisson and Nachmanshon 1949;Vigny et al 1978).…”

“…These two enzymes, AChE and ChE can be distinguished not only by their distribution but also by their substrate specificity and their sensitivity to certain selective inhibitors (Augustisson and Nachmanshon 1949;Davison 1955;Toutant et al 1985;Vigny et al 1978). Both AChE and ChE are inhibited by eserine but only AChE is inhibited by 1.5-bis(4-allyl dimethyl amino phenyl)pentan-3-one dibromide (BW284C51) and by an excess of substrate, for example acetylthiocholine chloride (ACh) (Augustisson and Nachmanshon 1949;Vigny et al 1978). These enzymes may be soluble, linked to the basal lamina via a collagen tail or to membrane via a glycolipid or via a hydrophobic peptide (Bon et al 1979;Massoulie and Bon 1982).…”