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Purification and Kinetics of Bovine Kidney Cortex Glutathione Reductase

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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; branched mechanism; kinetics; purification

Document Type: Research Article


Publication date: 2010-05-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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