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- W2044227890 abstract "Abstract Cu-thionein purified from rat liver contains 10 g atoms Cu per mole protein. EPR and NMR bulk susceptibility studies indicate that the copper ions are bound in a diamagnetic state. Purification of the metalloprotein anaerobically results in a sample in which 18 cysteines can be titrated by 2,2-dithiodipyridine. Only 10–12 cysteines could be titrated in aerobically prepared samples. The copper ions in aerobically prepared Cu-thionein are more easily removed by ethylenediaminetetraacetic acid and diethylenetriaminepentaacetic acid than are the ions in the anaerobically purified protein. Likewise, the Cu ions in aerobically prepared Cu-thionein molecules have the ability to reactivate aposuperoxide dismutase and to bind to apocarbonic anhydrase whereas the metal ions in anaerobically prepared Cu-thionein molecules do not. A qualitative correlation was found between the extent of sulfhydryl oxidation in Cu-thionein and the reactivity of thionein-bound Cu ions with chelators such as the apometalloenzymes. The reconstitution assay system represents a sensitive indicator of the reactivity of Cu-thionein. The results suggest that rat liver Cu-thionein is very susceptible to oxidation and the Cu-binding affinity varies accordingly." @default.
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- W2044227890 date "1982-01-01" @default.
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- W2044227890 title "Metal binding sites of rat liver Cu-thionein" @default.
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- W2044227890 doi "https://doi.org/10.1016/0003-9861(82)90445-3" @default.
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