Home
Deutsch
Advanced Search
Browse by ...
Publication overview
Contact persons
Help
PMC
 |
|
Open Access Green as soon as Postprint is submitted to ZB.
Metal-catalyzed inactivation of bovine glucose-6-phosphate dehydrogenase - role of thiols.
FEBS Lett. 396, 95-98 (1996)
The role of thiols as oxidant scavengers during inactivation of bovine glucose-6-phosphate dehydrogenase by metal-catalyzed oxidation systems has been studied in vitro. Partial inactivation of the enzyme was achieved by the metal-catalyzed oxidation systems Fe(II)/H202/EDTA or Fe(II)/H202/ADP under specific conditions. When EDTA as chelator was present in the oxidation system, both cysteine and N-acetylcysteine at low concentrations (0.1-1 mM) drastically enhanced inactivation, while cysteinyl-glycine and glutathione did not. The thiol-mediated inactivation was inhibitable by superoxide dismutase. Depletion of enzyme activity by cysteine was paralleled by an increase of the carbonyl content, which indicates oxidative injury. However, when EDTA as chelator was replaced by the natural chelator ADP, all thiols studied acted as antioxidants. It is therefore concluded that the nature of the chelator as a constituent of the metal-catalyzed oxidation systems determines whether the antioxidative function of some thiols is shifted to a prooxidative function against glucose-6-phosphate dehydrogenase.
Altmetric
Additional Metrics?
Edit extra informations
Login
Publication type
Article: Journal article
Document type
Scientific Article
ISSN (print) / ISBN
0014-5793
e-ISSN
1873-3468
Journal
FEBS Letters
Quellenangaben
Volume: 396,
Issue: 1,
Pages: 95-98
Publisher
Elsevier
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Lung Biology (LHI)