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The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.

Superoxide Dismutases: II. Purification and Quantitative Relationship with Water-soluble Protein in Seedlings

Open access
Giannopolitis, Constantine N., Ries, Stanley K.·1977·Plant Physiology

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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Crossref · 10.1104/pp.59.2.315

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Metadata

Authors
Giannopolitis, C. N., & Ries, S. K.
Venue
Plant Physiology
Published
1977-02-01
Volume
59
Issue
2
Pages
315-318
ISSN
  • 0032-0889 (ISSN-L)
  • 1532-2548
OpenAlex
W2023392223
Cited by
658
References
8
FWCI
0.00
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Superoxide Dismutases: II. Purification and Quantitative Relationship with Water-soluble Protein in Seedlings. https://app.cochat.ai/papers/10.1104/pp.59.2.315
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Giannopolitis, C. N., & Ries, S. K. (1977). Superoxide Dismutases: II. Purification and Quantitative Relationship with Water-soluble Protein in Seedlings. Plant Physiology. https://doi.org/10.1104/pp.59.2.315

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