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Studies on the Purification and Characterization of Superoxide Dismutase from Tartary Buckwheat Leaves

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Abstract

Copper and zinc-containing superoxide dismutase with high specific activity was prepared from fresh tartary buckwheat leaves. The molecular weight of the purified enzyme is about 31kD, a maximum UV-absorption of the enzyme is found at 259nm, and the analysis of amino acid composition showed that the enzyme contains 308 amino acid residues.The purified enzyme showed three isozyme bands by PAGE.

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Copper and zinc-containing superoxide dismutase with high specific activity was prepared from fresh tartary buckwheat leaves. The molecular weight of the purified enzyme is about 31kD, a maximum UV-absorption of the enzyme is found at 259nm, and the analysis of amino acid composition showed that the enzyme contains 308 amino acid residues.The purified enzyme showed three isozyme bands by PAGE.

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Available abstract

Copper and zinc-containing superoxide dismutase with high specific activity was prepared from fresh tartary buckwheat leaves. The molecular weight of the purified enzyme is about 31kD, a maximum UV-absorption of the enzyme is found at 259nm, and the analysis of amino acid composition showed that the enzyme contains 308 amino acid residues.The purified enzyme showed three isozyme bands by PAGE.

Key concepts: Superoxide dismutase, Enzyme, Isozyme, Chemistry, Zinc, Biochemistry, Amino acid, Enzyme assay

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