Thomas J A, Mallis R J
Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
Exp Gerontol. 2001 Sep;36(9):1519-26. doi: 10.1016/s0531-5565(01)00137-1.
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.
