- Collection:
- Atlanta University and Clark Atlanta University Theses and Dissertations
- Title:
- Glutathione s-transferase as a potential biomarker for organophosphate exposure
- Creator:
- Burton, Leslie J.
- Date of Original:
- 1996-12-01
- Subject:
- Degrees, Academic
Dissertations, Academic - Location:
- United States, Georgia, Fulton County, Atlanta, 33.749, -84.38798
- Medium:
- theses
- Type:
- Text
- Format:
- application/pdf
- Description:
- Three munition simulants were employed for the assessment of Glutathione S- Transferase (GST) as a biomarker of chemical munition exposure. Cell toxicity in human liver cells (HEP-G2), mutagenic capacity, and acetylcholinesterase inhibition have been demonstrated with these simulants (1) Y-glutamyl-a-amino-P-[(2-ethyl N,N,N',N'- tetraethylphosphorodiamidate)sulfonyl]propionylglycine (2) y-glutamyl-a-amino-P-[ [2- ethyl A(MMAr'-tetrakis(2-chloroethyl)phosphorodiamidate]sulfonyl]propionylglycine, (3) y -glutamyl-a-amino-P-[ [2-ethyl TV, N, Y'.TV'-tetraki s (2-chloroethyl)phosphoro- diamidate]sulfonyl]propionyl-(R)-(-)phenylglycine. In addition, GST was purified from human liver cells via elution on a S-hexylglutathione-bound agarose column. Elution yielded a high-affinity and low-affinity form of GST. Subsequent GST kinetic analysis with reduced glutathione, 1 -chloro-2,4-dinitrobenzene and the simulants suggested interaction via catalytic and non-catalytic sites. In addition, HPLC separation of tryptic digests of simulant-treated GST and untreated GST suggest that the enzyme is structurally modified in the presence of the simulants.
- External Identifiers:
- Metadata URL:
- http://hdl.handle.net/20.500.12322/cau.td:1996_burton_leslie_j
- Rights Holder:
- Clark Atlanta University
- Holding Institution:
- Atlanta University Center Robert W. Woodruff Library
- Rights:
-
