An organofluorophosphate-hydrolyzing activity in Tetrahymena thermophila

An enzymatic activity that hydrolyzes O,O-diisoproplyphosphofluoridate (DFP) and O-1,2,2-trimethylpropylmethylphosphonofluoridate (Soman) was discovered in the ciliate protozoan Tetrahymena thermophila. The enzymatic activity classifies the protein as Mazur-type similar to that found in hog kidney a...

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Bibliographic Details
Published inThe Journal of protozoology Vol. 32; no. 3; p. 517
Main Authors Landis, W G, Savage, Jr, R E, Hoskin, F C
Format Journal Article
LanguageEnglish
Published United States 01.08.1985
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Summary:An enzymatic activity that hydrolyzes O,O-diisoproplyphosphofluoridate (DFP) and O-1,2,2-trimethylpropylmethylphosphonofluoridate (Soman) was discovered in the ciliate protozoan Tetrahymena thermophila. The enzymatic activity classifies the protein as Mazur-type similar to that found in hog kidney and Escherichia coli. The rate of hydrolysis of Soman by the Tetrahymena-extract is the highest, on a per gram of extract basis, of any eucaryote. The molecular weight is approximately 75,400 as determined by Sephacryl column chromatography. A maximum fifteen-fold purification has been achieved. Potential exists for the detoxification and one-step detection of common organofluorophosphate pollutants. Additionally, Tetrahymena should prove an easier subject for manipulation than mammalian or squid sources. Protozoa may be a potentially important source of detoxification and degradation enzymes for other environmental contaminants.
ISSN:0022-3921
DOI:10.1111/j.1550-7408.1985.tb04053.x