ArticleThe protein journal2010
Purification and characterisation of rat kidney glutathione reductase.
Article in The protein journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Riboflavin intake and kidney health: population evidence and mechanistic insights from NHANES and molecular docking analyses.Renal failure · 2026Article
- Extracellular Vesicles, Nutrient Balance, and Redox Metabolism During Epididymal Sperm Maturation: A Perspective on the Complexity of Intercellular Interplay.Advances in anatomy, embryology, and cell biology · 2026Review
- Physiological Associations between Vitamin B Deficiency and Diabetic Kidney Disease.Biomedicines · 2023Review
- Regulation of Mitochondrial Hydrogen Peroxide Availability by Protein S-glutathionylation.Cells · 2022Review
- NOX-like ROS production by glutathione reductase.iScience · 2022Article
- Parallel molecular mechanisms for enzyme temperature adaptation.Science (New York, N.Y.) · 2021Article
- Assessing the Covalent Attachment and Energy Transfer Capabilities of Upconverting Phosphors With Cofactor Containing Bioactive Enzymes.Frontiers in chemistry · 2020Article
- A mechanistic model for thiol redox dynamics in the organogenesis stage rat conceptus.Reproductive toxicology (Elmsford, N.Y.) · 2018Article
- The Incomplete Glutathione Puzzle: Just Guessing at Numbers and Figures?Antioxidants & redox signaling · 2017Review
- Differential expression of disulfide reductase enzymes in a free-living platyhelminth (Dugesia dorotocephala).PloS one · 2017Article
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5 authors.
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Abstract
Glutathione reductase [GR, E.C.1.8.1.7] catalyses NADPH dependent reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH). Thus, it is the crucial enzyme to maintain high [GSH]/[GSSG] ratio and physiological redox status in cells. Kidney and liver tissues were considered as a rich source of GR. In this study, rat kidney GR was purified and some of its properties were investigated. The enzyme was purified 2,356 fold with a yield of 16% by using heat-denaturation and Sephadex G25 gel filtration, 2',5'-ADP Agarose 4B, PBE94 column chromatographies. The purified enzyme had a specific activity (Vm) of 250 U/mg protein and the ratio of absorbances at wavelengths of A (273)/A (463,) A (280)/A (460), A (365)/A (460), and A (379)/A (463), were 7.1, 6.8, 1.2 and 1.0, respectively. Each mol of GR subunit bound 0.97 mol of FAD. NADH was used as a coenzyme by rat kidney GR but with a lower efficiency (32.7%) than NADPH. Its subunit molecular weight was estimated as 53 kDa. An optimum pH of 6.5 and optimum temperature of 65 degrees C were found for rat kidney GR. Its activation energy (Ea) and temperature coefficient (Q(10)) were calculated as 7.02 kcal/mol and 1.42, respectively. The Km((NADPH)) and kcat/Km ((NADPH)) values were found to be 15.3 +/- 1.4 microM and 1.68 x 10(7) M(-1) s(-1) for the concentration range of 10-200 microM NADPH and when GSSG is the variable substrate, the Km((GSSG)) and the kcat/Km((GSSG)) values of 53.1 +/- 3.4 microM and 4.85 x 10(6) M(-1) s(-1) were calculated for the concentration range of 20-1,200 microM GSSG.
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