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This could explain why the activity of rhGPx3 mutant using H 2 O 2 as oxidizing substrate was in the same order of magnitude as that of human native GPx4 (34.8 U/mg) 9 and GPx4 mutant with all Cys converted to Ser (14.0 U/mg) 16 , while it was much lower than that of native GPx4 (64.6 U/mg) and the GPx4 mutant (24.6 U/mg) in the case of using PLPC-OOH as the oxidizing substrate

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