Thiols (RSH) may be subjected to oxidation reaction via oxidants and create disulfide (RSSR). Under conditions of oxidative stress, the oxidation of cysteine residues can lead to a reversible formation of disulfide bonds between protein thiol groups and low-molecular-mass thiols. These disulfide bonds can also be reduced back to thiol groups. This process thus maintains dynamic thiol-disulfide homeostasis, with itscrucial role in antioxidant protection and detoxification (17,18).No difference was determined between the groups in terms of native thiol, total thiol or thiol disulfide measurements in the present study. These findings also support the idea of good myocardial protection in the DNS group.