A comparison of the effects of ionic strength on three preparations of acetylcholinesterase in the presence and absence of gallamine

The kinetic behaviour of three forms of acetylcholinesterase as a function of ionic strength of the medium was investigated. The forms of enzyme were that bound to human erythrocyte membranes, acetylcholinesterase solubilized from these by Triton X-100, and a commercial preparation of the enzyme from bovine erythrocytes. The properties investigated were hydrolysis of the substrate acetylthiocholine, decarbamylation of dimethylcarbamyl-acetylcholinesterase and ageing of isopropylmethylphosphonyl-acetylcholinesterase. The effect of 10^?5 M gallamine triethiodide on these properties was also examined as a function of ionic strength.Detailed results for the variation of kinetic behaviour with ionic strength and the presence of gallamine are presented. No unified theory to predict the influence of these variables on all three forms of the enzyme could be formulated. Thus, the enzyme conformation stabilized by gallamine at low ionic strength was not necessarily similar to that of the gallamine-free enzyme at physiological ionic strength. Nor was it useful to consider the free enzyme at low ionic strength to be a model of the membrane-bound enzyme in vivo (Crone, 1973).It was concluded that kinetic results for solubilized and partially or wholly purified acetylcholinesterase cannot be extrapolated to the membrane-bound enzyme. Prediction of the effect of drugs on the system in vivo requires the use of the membrane-bound enzyme.