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Occurrence of Glutathione-Modified Aldose Reductase in Oxidatively Stressed Bovine Lens
- Source :
- Biochemical and Biophysical Research Communications; February 15, 1995, Vol. 207 Issue: 2 p775-782, 8p
- Publication Year :
- 1995
-
Abstract
- The optimization of an affinity chromatography method on Matrex Orange resin allowed the separation of glutathione modified and native aldose reductase in crude extracts of bovine lens. The analysis of hyperbaric oxygen treated lenses revealed the formation in the intact cultured lens of an enzyme form displaying affinity column binding properties, specific activity, sensitivity to inhibition and susceptibility to activation by thiol reducing agents, all comparable to glutathione modified aldose reductase. The extent of the enzyme modification increased with the time of the oxidative treatment and was maximal in the lens nucleus. The relative increase of glutathione modified aldose reductase from cortex to the nucleus is consistent with the increase in these lens regions of the GSSG/GSH ratio.Copyright 1995, 1999 Academic Press, Inc.
Details
- Language :
- English
- ISSN :
- 0006291X and 10902104
- Volume :
- 207
- Issue :
- 2
- Database :
- Supplemental Index
- Journal :
- Biochemical and Biophysical Research Communications
- Publication Type :
- Periodical
- Accession number :
- ejs803814
- Full Text :
- https://doi.org/10.1006/bbrc.1995.1254