ID | 62 |
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Name | glutathione reductase |
Synonyms | GLUR; GR; GRD 1; GRD1; GRase; GSR; Glutathione reductase; GRases… |
ID | 1341 |
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Name | rotenone |
CAS |
PubMed | Abstract | RScore(About this table) |
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1584202 | Peinado J, Florindo J, Lopez-Barea J: Glutathione reductase from Saccharomyces cerevisiae undergoes redox interconversion in situ and in vivo. Mol Cell Biochem. 1992 Mar 25;110(2):135-43. Redox interconversion of glutathione reductase was studied in situ with S. cerevisiae. The enzyme was more sensitive to redox inactivation in 24 hour-starved cells than in freshly-grown ones. While 5 microM or 100 microM caused 50% inactivation in normal cells in 30 min, 0.75 microM or 50 microM promoted a similar effect in starved cells. reactivated the enzyme previously inactivated by ascertaining that the enzyme was subjected to redox interconversion. Low EDTA concentrations fully protected the enzyme from inactivation, thus confirming the participation of metals in such a process. Extensive inactivation was obtained in permeabilized cells incubated with or in agreement with the very high specific activities of the corresponding dehydrogenases. Some inactivation was also observed with L-lactate, or in the presence of low concentrations. The inactivation of yeast glutathione reductase has also been studied in vivo. The activity decreased to 75% after 2 hours of growth with as carbon source, while rose to 144% and fell to 86% of their initial values. Greater changes were observed in the presence of 1.5 microM rotenone: enzymatic activity descended to 23% of the control value, while the /NAD+ and / ratios rose to 171% and 262% of their initial values, respectively. Such results indicate that the lowered redox potential of the nucleotide pool existing when is oxidized promotes in vivo inactivation of glutathione reductase. |
4(0,0,0,4) |