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Inhibitory effect of N-ethylmaleimide in two types of glutathione reductases

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F12%3A39895459" target="_blank" >RIV/00216275:25310/12:39895459 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Inhibitory effect of N-ethylmaleimide in two types of glutathione reductases

  • Original language description

    Glutathione reductase (GR) is a key enzyme of glutathione metabolism. This enzyme catalyzes the NADPH-dependent reduction of glutathione disulfide to a reduced form. The aim of the described study was to estimate an enzyme inhibition in two types of glutathione reductases (human and yeast) through Nethylmaleimide (NEM). The glutathione reductase activity was determined by the spectrophotometric method based on the measurement of an absorbance decline (8 = 340 nm) due to oxidation of NADPH. Interestingly, it was found that the presence of 100 :M NEM had no effect in the two glutathione reductases. The inhibitory effect was proved in higher concentrations of N-ethylmaleimide; however, neither 2 mM NEM was able to diminish GR activity. The enzyme activitywas reduced in both GRs; the human GR was inhibited by 15 % and 37 % in the presence of 1 mM and 2 mM NEM, respectively; the yeast GR was inhibited at the same concentrations of N-ethylmaleimide by 16 % and 35 %, respectively. We assesse

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    ED - Physiology

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2012

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Scientific Papers of the University of Pardubice, Series A, Faculty of Chemical Technology

  • ISSN

    1211-5541

  • e-ISSN

  • Volume of the periodical

    18

  • Issue of the periodical within the volume

    prosinec

  • Country of publishing house

    CZ - CZECH REPUBLIC

  • Number of pages

    7

  • Pages from-to

    29-35

  • UT code for WoS article

  • EID of the result in the Scopus database