Kinetics of the DFPase activity in Tetrahymena thermophila.

作者: WAYNE G. LANDIS , MARK V. HALEY , DENNIS W. JOHNSON

DOI: 10.1111/J.1550-7408.1986.TB05593.X

关键词:

摘要: Crude homogenates of the ciliate protozoon, Tetrahymena thermophila, can hydrolyze potent acetylcholinesterase inhibitors O,O-diisopropylphosphorofluoridate (DFP) and O-1,2,2-trimethylpropylmethylphosphonofluoride (soman). Characterization enzymatic activity homogenate has been performed. The DFPase operates over a pH range 4 to 10 an ionic 0-500 mM NaCl. Rate reaction increases three- four-fold from 25 degrees C 40 is still present at 55 C. These results indicate that broad environmental conditions, making it attractive material for use in detoxification detection organofluorophosphates. DFPases may be important metabolism naturally occurring organophosphates.

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