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- W1990216696 abstract "The role of thioredoxin in the reduction of protein mixed disulfides (dethiolation) was studied by electrofocusing methodology with glycogen phosphorylase b and creatine kinase as substrates for the reaction. Glycogen phosphorylase b was effectively dethiolated by Escherichia coli thioredoxin with dithiothreitol as the reductant, while creatine kinase could not be dethiolated by this mechanism. The rate of dethiolation of phosphorylase b was dependent on the concentration of thioredoxin up to a maximum at 20 microM when the concentration of phosphorylase b was 4 microM in monomer. Rat heart contained a thioredoxin reductase activity that could use added E. coli thioredoxin to dethiolate phosphorylase b and the same concentration of thioredoxin as above was required. This activity was not expressed with creatine kinase as the substrate. Cardiac tissue was shown to have a similar endogenous dethiolating activity. These results suggest that thioredoxin may play an important role in dethiolating specific proteins that might become S-thiolated during oxidative stress of cardiac tissue." @default.
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- W1990216696 date "1989-07-01" @default.
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- W1990216696 title "Reduction of protein mixed disulfides (Dethiolation) by Escherichia coli thioredoxin: A study with glycogen phosphorylase b and creatine kinase" @default.
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- W1990216696 doi "https://doi.org/10.1016/0003-9861(89)90190-2" @default.
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