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Plant Physiology 78:357-358 (1985)
© 1985 American Society of Plant Biologists

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Articles

Superoxide Dismutase from Lens esculenta

Purification and Properties

Rodolfo Federico, Rosaria Medda and Giovanni Floris

Dipartimento Biologia Vegetale, Città Universitaria 00185 Roma, Italy, Istituto di Chimica Biologica, via Della Pineta 77, 09100 Cagliari, Italy

Superoxide dismutase has been purified to homogeneity from Lens esculenta cotyledons and shoots. The two forms appeared to be identical. The purified enzyme contained two electrophoretically distinct bands. It contained two ions of Cu and two ions of Zn. Gel filtration experiments indicate a molecular weight of about 33,000. The spectrum of ultraviolet and visible regions and electron paramagnetic resonance were similar to those of Cu-Zn mammalian superoxide dismutase.






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Copyright © 1985 by the American Society of Plant Biologists