Competition of the Aliesterase in Rat Serum with the Pseudo Cholinesterase for Diisopropyl Fluorophosphonate

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Abstract
The molar concn. of pseudocholinesterase in certain mammalian sera can be determined by the use of a competitive reversible inhibitor, Nu-683, the dimethyl carbamate of tri-methylammonium bromide, and an analog of prostigmine. It is known that diisopropyl fluorophosphate (DFP) is a moderately potent inhibitor of hydrolytic enzymes other than the cholinesterases, and it has been reported previously that the aliesterases of rat serum show an abnormally high snesitivity to DFP. The present series of expts. lead to the conclusion that the high concn. of DFP necessary to inhibit the pseudocholinesterase in normal rat serum is due, in part at least, to the fact that the DFP combines preferentially with other proteins in the serum[long dash]namely the aliesterase.