Identification, Purification, and Partial Characterization of the GV- Degrading Enzyme from ATCC No. 29660 Alteromonas Undina

摘要

The GV (2-dialkylaminoalkyl N,N-dialkylphospho namidofluoridate) nerve agent has a toxicity intermediate to G and V-type nerve agents and is not catalyzed by either organophosphorus acid anhydrolases (OPAA) or organophosphorus hydrolase (OPH) enzymes. We have screened and identified a number of Alteromonas strains possessing catalytic activity using a GV compound as substrate. The enzyme from one of these strains, A. undina, has been purified to homogeneity by ammonium sulfate fractionation and Q Sepharose anion exchange chromatography. The activity of GV-hydrolyzing enzyme peak is distinct from that of A. undina OPAA following the Q Sepharose column chromatography. The SDS- polyacrylamide gel electrophoresis of the GV-hydrolyzing enzyme fraction revealed a single polypeptide of (caret) 20kDa. To our knowledge, this is the first report of enzymatic detoxification of GV.