There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.
Abstract
Protein sulfhydryls are potential sites of reversible oxidative modification by S-glutathiolation,
and S-nitrosylation, but they are also susceptible to irreversible damage by oxidative
conditions. In the absence of adequate antioxidant protection, these reactive sites
may become useless because of this irreversible damage. It has recently become possible
to directly access the nature and amount of irreversibly oxidized protein sulfhydryls
by both gel-based methods and direct amino acid analysis. Results are in keeping with
the concept that irreversible oxidation of protein sulfhydryls is more extensive in
aged tissue samples. It is proposed that an adequate pool of glutathione is essential
to prevent this increase in sulfhdryl oxidation. The increased amount of protein sulfhydryl
damage may be critically important to the function of signal-transduction and transcription
events that utilize proteins containing these reactive sites.