Abstract
In Pisum sativum, about 90% of the glutathione in leaf and root is in the reduced form. GSSG reductase has been purified from chloroplasts and roots. The two enzymes had similar M,s, but differed in pH optimum and sensitivity to inhibition by zinc, copper and ferrous ions. In comparison with the oxidized form, the reduced form of the enzymes had a much greater temperature instability, and was inhibited by N-ethyl maleimide.
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