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J. Biol. Chem., Vol. 260, Issue 29, 15394-15397, Dec, 1985
K Kim, SG Rhee and ER Stadtman
Many enzymes, represented by yeast glutamine synthetase, are inactivated
and degraded in the presence of dithiothreitol (DTT), oxygen, and catalytic
amounts of iron salts. The roles of DTT and iron can be replaced by
ascorbate and copper, respectively. Experimental data suggest that reactive
oxygen species, likely hydroxyl radicals, are generated locally around
irons bound at specific sites on enzymes, and these species are responsible
for the inactivation and degradation. Since many biochemicals are
contaminated with metal salts in quantities sufficient for some hydroxyl
radical formation to occur, the possibility of oxidative modification and
degradation should be considered when an enzyme is exposed to DTT.
Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron
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