The interaction of organophosphate and carbamate insecticides with cholinesterases in the terrestrial pulmonate, Limax maximus

Isaac N Pessah, Phillip G. Sokolove

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

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 languageEnglish (US)
Pages (from-to)291-297
Number of pages7
JournalComparative Biochemistry and Physiology. Part C, Comparative
Volume74
Issue number2
DOIs
StatePublished - 1983
Externally publishedYes

Fingerprint

Carbamates
Organophosphates
Cholinesterases
Insecticides
Hemolymph
Methiocarb
Foot
Carbaryl

ASJC Scopus subject areas

  • Immunology
  • Pharmacology

Cite this

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abstract = "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.",
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AB - 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.

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