SGD Paper 
Hospodar'ov DV, et al. (2005) [Free radical inactivation of glucose-6-phosphate dehydrogenase in Saccharomyces cerevisiae in vitro] Ukr Biokhim Zh 77(1):58-64
Abstract: Partial purification and in vitro inactivation of glucose-6-phosphate dehydrogenase from the yeast Saccharomyces cerevisiae in the Fe2+/H2O2 oxidation system were conducted. At the protein concentration 1.5 mg/ml, the enzyme lost 50% of activity within 5 minutes of incubation in presence of 2 mM hydrogen peroxide and 3 mM ferrous sulphate. The inactivation extent depended on time and concentrations of FeSO4 and H2O2. EDTA, ADP and ATP at concentration 0.5 mM enhanced inactivation. At the same time, the presence of 0.5 mM NADPH, 1 mM glucose-6-phosphate, 10 mM mannitol, 30 mM dimethylsulphoxide or 20 mM urea diminished this process. In comparison with native enzyme, index S(0,5) of the partially inactivated enzyme for glucose-6-phosphate was 2.1-fold higher, but for NADP it was 1,6-fold lower. Maximal activity of the partially inactivated enzyme was 3-5-fold lower than that of native one.FAU - Hospodar'ov, D .
| Status: Published | Type: Journal Article | PubMed ID: 16335270 |
Topics addressed in this paper
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.
| Topics | Genes linked to topics |
|---|---|
| ZWF1 | |
| Mutants/Phenotypes |  |
| Primary Literature | |
| Protein Physical Properties | |
| Protein Processing/Modification/Regulation | |
