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Selective Evaluation of Thioredoxin Reductase Enzymatic Activities

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Selenoproteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1661))

Abstract

Thioredoxin reductases are important oxidoreductases that keep the active site disulfide/dithiol motif of thioredoxins reduced using NADPH, thereby supporting many thioredoxin-dependent reductive pathways in cells. Mammalian thioredoxin reductases are selenoproteins that have several additional substrates beyond thioredoxins. This chapter first lists several different assays for measurement of thioredoxin reductase activities, before giving a protocol for a selective evaluation of these activities that can be used in either crude cell lysates as well as with purified enzymes. The same assay can also be easily adopted for the determination of thioredoxin activities.

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Acknowledgments

The author acknowledges funding from The Swedish Cancer Society, The Swedish Research Council, Swedish Foundation for Strategic Research, Knut and Alice Wallenberg Foundation, and Karolinska Institutet.

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Authors and Affiliations

  1. Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, 171 77, Stockholm, Sweden

    Elias S. J. Arnér

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  1. Elias S. J. Arnér
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Correspondence to Elias S. J. Arnér .

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Editors and Affiliations

  1. Centre International de Recherche en Infectiologie, CIRI, Lyon, France

    Laurent Chavatte

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Arnér, E.S.J. (2018). Selective Evaluation of Thioredoxin Reductase Enzymatic Activities. In: Chavatte, L. (eds) Selenoproteins. Methods in Molecular Biology, vol 1661. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7258-6_21

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  • DOI: https://doi.org/10.1007/978-1-4939-7258-6_21

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-7257-9

  • Online ISBN: 978-1-4939-7258-6

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