A spectrophotometric glutathione S-transferase assay displaying alpha-class selectivity utilizing 1-p-chlorophenyl-4,4-dimethyl-5-diethylamino-1-penten-3- one hydrobromide.
Journal Article (Journal Article)
The conjugation of 1-p-chlorophenyl-4,4-dimethyl-5-diethylamino-1-penten-3- one hydrobromide (CDDP), a Mannich base of an alpha,beta-unsaturated ketone, to glutathione is catalyzed selectively by alpha-class glutathione S-transferase. The reaction of CDDP with glutathione can be monitored continuously by following the conjugation-dependent decrease in absorbance of CDDP at 307 nm. The Km and Vmax for CDDP with alpha-class glutathione S-transferase from horse liver were determined to be 226 microM and 14.6 mumol/(min.mg), respectively. CDDP is the first example of an alpha-class glutathione S-transferase selective substrate that monitors the glutathione conjugation activity, rather than the glutathione peroxidase activity of the enzyme.
Full Text
Duke Authors
Cited Authors
- Sexton, DJ; Dimmock, JR; Mutus, B
Published Date
- 1993
Published In
Volume / Issue
- 71 / 1-2
Start / End Page
- 98 - 101
PubMed ID
- 8329183
International Standard Serial Number (ISSN)
- 0829-8211
Digital Object Identifier (DOI)
- 10.1139/o93-016
Language
- eng
Conference Location
- Canada