Literature DB >> 4999483

Species specificity of phosphate triester anticholinesterases.

C Donninger.   

Abstract

Two widely distributed enzyme systems degrade phosphate triester anticholinesterase agents to inactive phosphate diesters by nonhydrolytic mechanisms. The substrate specificity of these enzymes is discussed and the level of activity in various mammalian livers is described. The distribution of these enzymes is an important factor in accounting for the species specificity of at least some anticholinesterase agents.

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Year:  1971        PMID: 4999483      PMCID: PMC2428029     

Source DB:  PubMed          Journal:  Bull World Health Organ        ISSN: 0042-9686            Impact factor:   9.408


  2 in total

1.  Nature of a soluble, glutathione-dependent enzyme system active in cleavage of methyl parathion to desmethyl parathion.

Authors:  J I Fukami; T Shishido
Journal:  J Econ Entomol       Date:  1966-12       Impact factor: 2.381

2.  The metabolism of 2-chloro-1-(2',4'-dichlorophenyl)vinyl diethyl phosphate (Chlorfenvinphos) in the dog and rat.

Authors:  D H Hutson; D A Akintonwa; D E Hathway
Journal:  Biochem J       Date:  1967-01       Impact factor: 3.857

  2 in total

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