[Comparative analysis of sensitivity of cholinesterases of various origin to monoonium reversible inhibitors].

Analytical review of literature data has been presented about constants of interaction of cholinesterases of various animals (verterbrates and squids) with 89 onium (ammonium, phosphonium, and sulfonium) reversible inhibitors forming homologous series with regularly changed structure. Values of competitive, uncompetitive, and generalized inhibition constants have been compared. On this basis, conclusions are made about mechanism of action of the studied compounds and the predominant areas of their sorption--in the <<anionic>> or peripheral <<anionic>> sites of the enzymes. The presented data are discussed from the point of view of comparative biochemistry and in the light of the current information about structure of the cholinesterase active center.