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Biosensors and Bioelectronics, 1995 Proteins isolated from extreme thermophilic microorganisms for their general stability to the common protein denaturants (heating, pH, organic solvents, urea, SDS, proteases) represent an important development in the potential exploitation of proteins ...
Carlo A Raia +2 more
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Preparation and assay of mammalian thioredoxin and thioredoxin reductase
1999Publisher Summary This chapter describes the preparation and assay of mammalian thioredoxin and thioredoxin reductase (TrxR). The amino acid sequences of mammalian TrxR revealed a strikingly high homology to glutathione reductase. 14,19 The conserved features of all the structural components of glutathione reductase are preserved in mammalian TrxR ...
E S, Arnér, L, Zhong, A, Holmgren
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Kinetics of electron transfer from thioredoxin reductase to thioredoxin
Biochemistry, 1991The reduction of Escherichia coli thioredoxin by thioredoxin reductase was studied by stopped-flow spectrophotometry. The reaction showed no dependence on thioredoxin concentration, indicating that complex formation was rapid and occurred during the dead time of the instrument.
J A, Navarro +5 more
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Rat liver thioredoxin and thioredoxin reductase: purification and characterization
Biochemistry, 1982A reproducible scheme has been developed for the preparation of rat liver thioredoxin and thioredoxin reductase (EC 1.6.4.5) by using assays based on reduction of insulin and 5,5'-dithiobis(2-nitrobenzoic acid), respectively. Both proteins were purified to homogeneity, as judged from polyacrylamide gel electrophoresis.
M, Luthman, A, Holmgren
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Rhodanese as a thioredoxin oxidase
The International Journal of Biochemistry & Cell Biology, 2000A major catalytic difference between the two most common isoforms of bovine liver mitochondrial rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) has been observed. Both isoforms were shown to be capable of using reduced thioredoxin as a sulfur-acceptor substrate.
D L, Nandi, P M, Horowitz, J, Westley
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The thioredoxin system in cancer
Seminars in Cancer Biology, 2006Thioredoxin (Trx), NADPH and thioredoxin reductase (TrxR) comprise a thioredoxin system which exists in nearly all living cells. It functions in thiol-dependent thiol-disulfide exchange reactions crucial to control of the reduced intracellular redox environment, cellular growth, defense against oxidative stress or control of apoptosis and has multi ...
Elias S J, Arnér, Arne, Holmgren
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Biochemistry, 2010
The enzymatic activity of thioredoxin reductase enzymes is endowed by at least two redox centers: a flavin and a dithiol/disulfide CXXC motif. The interaction between thioredoxin reductase and thioredoxin is generally species-specific, but the molecular aspects related to this phenomenon remain elusive.
Oliveira, Marcos A. +5 more
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The enzymatic activity of thioredoxin reductase enzymes is endowed by at least two redox centers: a flavin and a dithiol/disulfide CXXC motif. The interaction between thioredoxin reductase and thioredoxin is generally species-specific, but the molecular aspects related to this phenomenon remain elusive.
Oliveira, Marcos A. +5 more
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Crystal Structure of the Plasmodium falciparum Thioredoxin Reductase–Thioredoxin Complex
Journal of Molecular Biology, 2013Over the last decades, malaria parasites have been rapidly developing resistance against antimalarial drugs, which underlines the need for novel drug targets. Thioredoxin reductase (TrxR) is crucially involved in redox homeostasis and essential for Plasmodium falciparum. Here, we report the first crystal structure of P.
Fritz-Wolf, K. +6 more
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