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. 1977 Feb;59(2):315–318. doi: 10.1104/pp.59.2.315

Superoxide Dismutases

II. Purification and Quantitative Relationship with Water-soluble Protein in Seedlings 1,2

Constantine N Giannopolitis a, Stanley K Ries a
PMCID: PMC542388  PMID: 16659840

Abstract

Superoxide dismutase was purified from pea (Pisum sativum L., cv. Wando) seeds and corn (Zea mays L., cv. Michigan 500) seedlings. The purified pea enzyme eluting as a single peak from gel exclusion chromatography columns contained the three electrophoretically distinct bands of superoxide dismutase characterizing the crude extract. The purified corn enzyme eluted as the same peak as the pea enzyme, and contained five of the seven active bands found in the crude extract. The similar molecular weights and the cyanide sensitivities of these bands indicated that they are probably isozymes of a cupro-zinc superoxide dismutase. One of the remaining corn bands was shown to be a peroxidase.

Superoxide dismutase accounted for 1.6 to 2.4% of the water-soluble protein in seedlings of corn, peas, and oats (Avena sativa L., cv. Au Sable). The superoxide dismutase activity per plant and per milligram water-soluble protein considerably increased during germination of oats and during greening and hook opening of peas.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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