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Glutathione is also a constituent in the regulation of protein and gene expression, exchange reactions including thiol to disulfide ratios involve glutathione.[4] Glutathione can exist intracellularly in either an oxidized (glutathione disulfide) or reduced (glutathione) molecular state

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164 Some studies have proposed that a fraction of the AAT protein is S-nitrosylated under physiological conditions, and that AAT nitrosylation is more efficient than the nitrosylation of bovine serum albumin or glutathione

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difficile by the production of a narrow-spectrum bacteriocin that disrupts the target bacterial cell membrane (Rea et al