PMID: 2097819Dec 1, 1990Paper

Molecular properties and inhibition kinetics of acetylcholinesterase obtained from rat brain and cockroach ganglion

Toxicology and Industrial Health
A K Singh

Abstract

1. The molecular composition of acetylcholinesterase (AChE) obtained from cockroach neural, and rat brain tissues was different. Vertebrate enzyme exhibited a higher degree of polymerization than insect enzyme. 2. Acephate was a potent inhibitor of cockroach AChE, but a poor inhibitor of rat AChE. Unlike acephate, methamidophos was a potent inhibitor of both cockroach and rat enzymes. Acephate exhibited greater affinity for the cockroach-AChE than for the rat-AChE, and acephate phosphorylated the cockroach-AChE several times faster than the rat enzyme. The rate of phosphorylation of insect and rat AChE was similar in the presence of methamidophos. Solubilization of AChE by Triton X-100 altered the kinetics of inhibition of rat AChE by acephate. However, solubilization did not alter the kinetics of inhibition of rat AChE by methamidophos or the kinetics of inhibition of cockroach AChE by acephate or methamidophos. 3. The mechanism of acephate-cockroach AChE interaction was different than the mechanism of acephate-rat AChE interaction. It is proposed that both the rat and cockroach enzyme may contain, along with the anionic and esteratic sites, an "electron deficient" (ED) binding site which may exhibit selectivity for acephate a...Continue Reading

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