Activity of Organophosphate Acid Anhydrase in Rangia cuneata.

Abstract

Enzymes capable of hydrolyzing diisopropyl fluorophosphate (DFP) and related acetylcholinesterase inhibitors, have been reported in the tissues of many animals and have recently been renamed as organophosphate acid (opa) anhydrases. Purified clam-digestive gland was used to individually test substrate solutions of DFP and Mipafox for (opa) anhydrase activity. Results indicate three groups of molecular weight-estimates for substrate-specific enzymes within R. cuneata. When DFP was substrate, proteins in the 73,447 to 81,991 D and 20,157 opa anhydrases ranging in weight from 105,026 to 138,286 D were discovered. This data suggests multiple enzymes within R. cuneata that are strictly characterized according to substrate specificity and molecular weight.

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Document Details

Document Type
Technical Report
Publication Date
Jan 01, 1988
Accession Number
ADA188864

Entities

People

  • Nancy A. Chester
  • Wayne G. Landis

Organizations

  • Edgewood Chemical Biological Center

Tags

DTIC Thesaurus Topics

  • Abstracts
  • Chemical Synthesis
  • Chemistry
  • Classification
  • Ecotoxicology
  • Enzyme Inhibitors
  • Enzymes
  • Escherichia Coli
  • Hydrolysis
  • Inhibition
  • Inhibitors
  • Lepidoptera
  • Molecular Weight
  • Organophosphates
  • Security
  • Substrates
  • Tissue Extracts

Readers

  • Aquatic Ecology
  • Molecular Genetics
  • Neurotoxicology