1. The interaction of cholinesterases from L. maximus muscular foot and hemolymph with several toxicologically relevant carbamates and organophosphates was explored. 2. Biomolecular rate constants of inhibition indicate that, among the carbamates, those of low toxicity such as dioxacarb and carbaryl exhibit a differential pattern of inhibition in the supernatant of a 110,000 g preparation of the muscular foot when compared to whole hemolymph cholinesterase. 3. This is in contrast to the inhibition exhibited by more molluscicidal carbamates such as methiocarb which shows similar rate constants of inhibition in both tissues. 4. Quantitation of the behavioral response to intoxication is presented and the possible contribution of differential inhibition of cholinesterases in L. maximus is discussed.
|Original language||English (US)|
|Number of pages||7|
|Journal||Comparative Biochemistry and Physiology. Part C, Comparative|
|State||Published - 1983|
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