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These results suggest that lower than normal glutathione reductase activity is sufficient to maintain GSH levels.
The irreversible oxidation of glutathione to glutathione sulfonic acid could be detected after 30 min exposure of glutathione to 40 mM H2O2 at 20 degrees C. A peak consistent with glutathione-sulfinic acid was transiently present, suggesting this compound behaved as an oxygen consuming antioxidant.
These findings indicate that factors regulating plasma glutathione concentration are complex and not simply related to dietary glutathione intake or supply of precursor amino acids.
The findings indicate that the monomethyl and monoethyl esters of glutathione are transported into cells and hydrolyzed to glutathione.
The relatively small increase of glutathione amount in the presence of oxidative and electrophilic agents compared to other thiol reactive agents is not due to increased GT degradation of glutathione.
Our results indicate that the measurement of glutathione recovery rate after CDNB treatment can be used to estimate de novo synthesis of glutathione.
The extracellular glutathione levels were increased at that time, suggesting the efflux of glutathione.
Blood glutathione is not a good measure of organ glutathione stores when dealing with indirect‐acting glutathione‐depleting substances.
Cysteine derived from the cleavage of extracellular glutathione can be used to maintain intracellular levels of glutathione.
This suggest that osmotic depletion of glutathione is not due to cellular efflux of intact glutathione.