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

Authors :
Anderson RS
Durst HD
Landis WG
Source :
Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology [Comp Biochem Physiol C Comp Pharmacol Toxicol] 1988; Vol. 91 (2), pp. 575-8.
Publication Year :
1988

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.

Details

Language :
English
ISSN :
0742-8413
Volume :
91
Issue :
2
Database :
MEDLINE
Journal :
Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology
Publication Type :
Academic Journal
Accession number :
2905972
Full Text :
https://doi.org/10.1016/0742-8413(88)90080-1