Literature DB >> 2905972

Organofluorophosphate-hydrolyzing activity in an estuarine clam, Rangia cuneata.

R S Anderson1, H D Durst, W G Landis.   

Abstract

1. The bivalve Rangia cuneata can enzymatically detoxify the organophosphorus acetylcholinesterase inhibitors DFP and soman. 2. Digestive gland homogenates contained Mazur-type DFPases based on response to Mn2+ ions, and relative rates of DFP: soman hydrolysis. Squid-type DFPase contributed little to the total organophosphate acid (OPA) anhydrase activity of these preparations. 3. The natural substrate(s) and physiological role(s) of OPA anhydrase in R. cuneata has yet to be determined; however, DFPase specific activity was pronounced in the digestive gland, the primary organ involved in bioconcentration and biotransformation of xenobiotics, and in the gills, which are in continuous contact with water-borne chemicals.

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Year:  1988        PMID: 2905972     DOI: 10.1016/0742-8413(88)90080-1

Source DB:  PubMed          Journal:  Comp Biochem Physiol C Comp Pharmacol Toxicol        ISSN: 0742-8413


  2 in total

1.  Purification and Properties of a Highly Active Organophosphorus Acid Anhydrolase from Alteromonas undina.

Authors:  T C Cheng; S P Harvey; A N Stroup
Journal:  Appl Environ Microbiol       Date:  1993-09       Impact factor: 4.792

2.  Transfer and expression of an organophosphate insecticide-degrading gene from Pseudomonas in Drosophila melanogaster.

Authors:  J P Phillips; J H Xin; K Kirby; C P Milne; P Krell; J R Wild
Journal:  Proc Natl Acad Sci U S A       Date:  1990-10       Impact factor: 11.205

  2 in total

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