Abstract
For the past two decades it has been known that several of the glutathione S-transferase (GST) isozymes are efficient at catalyzing the conjugation of electrophilic carcinogen and drug metabolites to the cellular nucleophile, glutathione. 1 - 2 Underlying these biochemical observations has been the assumption that conjugation of electrophiles to glutathione, with the concomitant decrease in alkylation of alternate sites in the cell, is an important event in protecting a cell and maintaining the integrity of its genome. 3 - 4.
| Original language | English |
|---|---|
| Title of host publication | Structure and Function of Glutathione S-Transferases |
| Publisher | CRC Press |
| Pages | 237-247 |
| Number of pages | 11 |
| ISBN (Electronic) | 9781040900758 |
| ISBN (Print) | 9781003760146 |
| DOIs | |
| State | Published - Jan 1 2026 |
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