Abstract
Glutathione reductase was purified 34806-fold with a final yield of 85 % from the bovine kidney cortex. Some molecular and kinetic properties of purified enzyme are investigated. Product inhibition studies showed that the enzyme obeys ‘branched’ mechanism: KmNADPH 18 ± 3 μM and KmGSSG 65 ± 5 μM were determined.
Keywords: Glutathione reductase, purification, kinetics, branched mechanism
Protein & Peptide Letters
Title: Purification and Kinetics of Bovine Kidney Cortex Glutathione Reductase
Volume: 17 Issue: 5
Author(s): Berivan Tandogan and N. Nuray Ulusu
Affiliation:
Keywords: Glutathione reductase, purification, kinetics, branched mechanism
Abstract: Glutathione reductase was purified 34806-fold with a final yield of 85 % from the bovine kidney cortex. Some molecular and kinetic properties of purified enzyme are investigated. Product inhibition studies showed that the enzyme obeys ‘branched’ mechanism: KmNADPH 18 ± 3 μM and KmGSSG 65 ± 5 μM were determined.
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Cite this article as:
Tandogan Berivan and Ulusu N. Nuray, Purification and Kinetics of Bovine Kidney Cortex Glutathione Reductase, Protein & Peptide Letters 2010; 17 (5) . https://dx.doi.org/10.2174/092986610791112684
DOI https://dx.doi.org/10.2174/092986610791112684 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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