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

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.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Giannopolitis CN,Ries SK

doi

10.1104/pp.59.2.315

subject

Has Abstract

pub_date

1977-02-01 00:00:00

pages

315-8

issue

2

eissn

0032-0889

issn

1532-2548

journal_volume

59

pub_type

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