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- W2095365226 abstract "The autooxidation of cysteine and homocysteine to their disulfide forms was determined by measuring the time course of thiol groups disappearance. We found the oxidative chemistry of cysteine and homocysteine to be quite different. In the absence of added Cu(II), cysteine autooxidized at a slower rate than homocysteine, though in its presence cysteine oxidation was much faster, homocysteine being found to be a poor responder to copper catalysis. Albumin speeded up the spontaneous oxidation of both aminothiols, the reaction being faster with cysteine than with homocysteine. The copper content of different albumins was found to be highly variable, ranging from 12.75 to 0.64 microg Cu(II)/g albumin. We propose that copper bound to albumin possesses redox cycling activity to perform cysteine oxidation since: (i) copper elimination by copper chelators markedly reduces oxidation; and (ii) a positive correlation exists between the albumin copper content and the oxidation reaction rate." @default.
- W2095365226 created "2016-06-24" @default.
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- W2095365226 date "2004-11-01" @default.
- W2095365226 modified "2023-09-23" @default.
- W2095365226 title "Oxidation of cysteine and homocysteine by bovine albumin" @default.
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- W2095365226 doi "https://doi.org/10.1016/j.abb.2004.08.028" @default.
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