Identification, Purification, and Partial Characterization of the GV-Degrading Enzyme from ATCC # 29660 Alteromonas Undina
Abstract
The GV (2-dialkylaminoalkyl N,N-dialkylphosphonamidofluoridate) 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 ^ 20kDa. To our knowledge, this is the first report of enzymatic detoxification of GV.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 2002
- Accession Number
- ADA411415
Entities
People
- Steven P. Harvey
- Tu-chen Cheng
Organizations
- Edgewood Chemical Biological Center