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

Show simple item record Nýdlová, Erika Roušar, Tomáš 2020-05-13T18:45:38Z 2020-05-13T18:45:38Z 2012
dc.identifier.isbn 978-80-7395-577-9
dc.identifier.issn 1211-5541
dc.description.abstract 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 (λ = 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 activity was 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 assessed NEM-induced inhibition of the enzyme activity in the presence of 1 mM GSSG (glutathione disulfide) where both GRs were inhibited to a larger extent than in 9 mM GSSG. On the other hand, if glutathione reductase was incubated with NADPH, followed by addition of NEM, the enzyme activity disappeared to a much higher extent. After 2 minutes of incubation with NADPH, the activity of yeast glutathione reductase was inhibited by 70 % and 100 % in the presence of 0.1 mM and 1 mM NEM, respectively. en
dc.format p. 29–35
dc.language.iso en
dc.publisher University of Pardubice en
dc.relation.ispartof Scientific papers of the University of Pardubice. Series A, Faculty of Chemical Technology. 18/2012 en
dc.rights open access en
dc.title Inhibitory effect of N–ethylmaleimide in two types of glutathione reductases en
dc.type Article en
dc.peerreviewed yes en
dc.publicationstatus published en

This item appears in the following Collection(s)

Show simple item record

Search DSpace

Advanced Search


My Account