Plasmid Involvement in Parathion Hydrolysis by Pseudomonas diminuta

An organism identified as Pseudomonas diminuta was found to hydrolyze parathion. Cells grown for 48 h contained 3,400 U of parathion hydrolase activity per liter of broth. Expression of enzymatic activity was lost at a high frequency (9 to 12%) after treatment with mitomycin C. Hydrolase-negative derivatives were missing a plasmid present in the wild-type organism. The molecular mass of this plasmid (pCS1), as determined by electron microscopy, was about 44 x 10 daltons.