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Protein thiol groups are susceptible to oxidation by reactive oxygen species (
1
). The occurrence of a specific thiol modification named protein S-glutathionation has been proposed to protect proteins from oxidative damage owing to its reversible characteristics (
2
–
4
). In addition, S-glutathionation modulates protein functions including enzyme activity (
4
–
5
), cytoskeletal protein strength (
6
), hemoglobin-gelling activity (
7
), and chaperon activity (
8
). Because an increase in cellular glutathione (GSSG) level is correlated with the formation of S-glutathionated protein, a mixed-disulfide exchange reaction has been proposed to be responsible for this protein modification (
2
–
5
,
9
–
10
). However, glutathione (GSH) modified proteins are also formed under a circumstance without significant change in GSSG level (
11
–
12
), and a radical-initiated process has therefore also been proposed (
3
). S-Gluthionated hemoglobin formation owing to oxidative stress has been noted in the red blood cells from different species (
13
–
15
). There are a total of six cysteine residues in the human hemoglobin molecule, but two of them (β93 residues) are highly reactive (
16
) and can form mixed disulfide with GSH (
14
). However, the location of reactive cysteines in hemoglobin varies in different animal species. For example, the cysteines in chicken α-hemoglobin are more active than those in β hemoglobin (
15
).