Accession Number:

ADA411415

Title:

Identification, Purification, and Partial Characterization of the GV-Degrading Enzyme from ATCC # 29660 Alteromonas Undina

Descriptive Note:

Final rept. Oct 2000-Sep 2001

Corporate Author:

EDGEWOOD CHEMICAL BIOLOGICAL CENTER ABERDEEN PROVING GROUND MD

Personal Author(s):

Report Date:

2002-02-01

Pagination or Media Count:

21.0

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.

Subject Categories:

  • Chemical, Biological and Radiological Warfare

Distribution Statement:

APPROVED FOR PUBLIC RELEASE