Aging and reactivatability of plaice cholinesterase inhibited by soman and its stereoisomers.
A simple and rapid method to study aging of soman-inhibited cholinesterases was developed. The method was applied to study the aging characteristics of soman-inhibited cholinesterase from the muscles of the plaice (Pleuronectes platessa). The orientation of the soman molecule in the active site is decisive both for the rate of aging and the degree of reactivation of unaged enzyme, a conclusion reached by using soman stereoisomers. Fluoride ions were found to affect reactivatability as well as aging rate.
D000818:Animals; D002802:Cholinesterases / Q000378:metabolism*; D004355:Drug Stability; D005399:Fishes; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000201:enzymology*; D009943:Organophosphorus Compounds / Q000494:pharmacology*; D009994:Osmolar Concentration; D011485:Protein Binding; D012969:Sodium Fluoride / Q000494:pharmacology; D012999:Soman / Q000494:pharmacology*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D009943:Organophosphorus Compounds; D012969:Sodium Fluoride; D012999:Soman; D002802:Cholinesterases