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


  • eng

Conference Location

  • Canada