The inhibition of catalase by glutathione |
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Authors: | Yi Sun and Larry W. Oberley |
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Affiliation: | Radiation Research Laboratory, 14 Medical Laboratories, The University of Iowa, Iowa City, IA 52242, U.S.A. |
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Abstract: | Reduced glutathione (GSH) inhibited catalase activity in a dose-dependent manner. DL-dithiothreitol (DL-DTT) and dithioerythritol (DTE) also inhibited catalase activity. The inhibition of catalase by GSH and DL-DTT could be reduced by NADPH. Polyacrilamide gel electrophoresis demonstrated the inhibition was partially reversible. The inhibition of catalase by GSH appeared to be partly due to superoxide radicals, since it was inhibited by active manganese superoxide dismutase, but not by heat-inactivated enzyme. Other chemical species also appear to take part in the inhibition, but they could not be identified. |
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Keywords: | Free radicals Catalase Glutathione NADPH |
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