Ref ID : 4174
Wayne G. Landis, Russell E. Savage, Jr., and Francis C.G. Hoskin; An Organofluorophosphate-Hydrolyzing Activity in Tetrahymena thermophila. J.Protozool. 32(3):517-519, 1985
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An enzymatic activity that hydrolyzes O.O-diisopropylphosphofluoridate (DFP) and O-1,2,2-trimethylpropylmethyl-phosphonofluoridate (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 organofluorphosphate 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.