Abstract
Glutathione S-transferase (EC 2.5.1.18) has been implicated in the detoxification of drugs and atmospheric pollutants bearing an electrophylic group. The presence of glutathione S-transferase (GSH S-transferase) has been demonstrated for the first time in bovine ocular lens and cornea. The one major species of GSH S-transferase from bovine lens has been purified to homogeneity. The enzyme has a molecular weight of 49 000 and is a dimer of equal size subunits. Kinetic properties and substrate specificity of the enzyme have been studied. The lens GSH S-transferase is probably present as a single species which is highly deamidated but catalytically active. GSH S-transferase of bovine lens does not have any GSH-peroxidase (GSH-Px II) activity which has been shown to be present in rat liver GSH S-transferase.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 29-39 |
| Number of pages | 11 |
| Journal | Experimental Eye Research |
| Volume | 30 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1980 |
| Externally published | Yes |
Keywords
- bovine lens
- drug detoxication
- glutathione S-transferase
- glutathione peroxidase
- immunological properties
- purification
ASJC Scopus subject areas
- Ophthalmology
- Sensory Systems
- Cellular and Molecular Neuroscience