Effects of soman, VX and 5-(1,3,3-trimethyl)indolinyl-N,N-dimethyl carbamate on cholinesterase isoenzymes in mouse plasma

The 8 cholinesterase (ChE) isoenzymes were separated by polyacrylamide gel electrophoresis (PAGE) from mouse plasma. Among them, IIa, IIc and IIIb (20+/-5%) were acetylcholinesterases (EC 3.1.17, AChE) and the rest were butyrylcholinesterases (EC 3.1.18, BuChE). The effects of soman, VX and 5-(1,3,3-trimethyl) indolinyl-N,N-dimethyl carbamate (TIDC) on the isoenzymes were observed in vivo and in vitro. Soman showed a higher selective inhibition to AChE isoenzymes than VX and TIDC which both selectively acted on the BuChE isoenzymes. During PAGE, the activity of the isoenzymes inhibited by VX (sc 30 microg/kg) spontaneously increased from 7% to 50% and that inhibited by TIDC (ip 3 mg/kg) from 42% to 104%, but no reactivation occurred in those inhibited by soman (sc 50-200 microg/kg). In a few days after sc soman 100 microg/kg, the activities of the ChE isoenzymes recovered at different rates (I