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Plant Physiology 73:31-35 (1983)
© 1983 American Society of Plant Biologists

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Articles

Purification and Partial Characterization of a Genetically-Defined Superoxide Dismutase (SOD-1) Associated with Maize Chloroplasts 1

James A. Baum2, Joel M. Chandlee and John G. Scandalios3

Department of Genetics, North Carolina State University, Raleigh, North Carolina 27650

The chloroplast-associated form of superoxide dismutase from maize (Zea mays L.) (SOD-1) has been purified by a stepwise procedure consisting of (NH4)2SO4 fractionation, G-100 Sephadex gel filtration, DEAE-Sephacel chromatography, and hydroxylapatite chromatography. This procedure resulted in a single band on sodium dodecyl sulfate-polyacrylamide gels indicating that the preparation is homogeneous. The holoenzyme molecular weight was estimated at 31,000 to 33,000 by gel filtration. The subunit molecular weight of this dimeric protein was estimated at 14,500 on sodium dodecyl sulfate-polyacrylamide gels. Studies involving amino acid composition analysis, immunological cross-reactivity, in vitro subunit hybridizations, and H2O2 sensitivity indicate that SOD-1 differs significantly from SOD-2 and SOD-4, the other cupro-zinc forms of SOD from maize. The possible physiological role of SOD-1 within the chloroplast is discussed.

2 Present address: Department of Molecular and Population Genetics, University of Georgia, Athens, GA.

3 Send reprint requests to: J. G. Scandalios.

1 Supported in part by National Institutes of Health Research Grant GM-22733 to J. G. S. Paper No. 8744 of the Journal Series of the North Carolina Agricultural Research Service, Raleigh, NC.






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Copyright © 1983 by the American Society of Plant Biologists