Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 98:331-336 (1992)
© 1992 American Society of Plant Biologists

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Metabolism and Enzymology

Purification and Properties of Glyoxysomal Cuprozinc Superoxide Dismutase from Watermelon Cotyledons (Citrullus vulgaris Schrad) 1

Pablo Bueno and Luis A. del Río

Unidad de Bioquímica Vegetal, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Cientificas, Apdo. 419, E-18080 Granada, Spain

A glyoxysomal copper,zinc-containing superoxide dismutase (EC 1.15.1.1) was purified to homogeneity, for the first time, from watermelon cotyledons (Citrullus vulgaris Schrad.). The stepwise purification procedure consisted of acetone precipitation, batch anion-exchange chromatography, anion-exchange Fast Protein Liquid Chromatography and gel-filtration column chromatography. Pure copper,zinc-superoxide dismutase (Cu,Zn-SOD II) had a specific activity of 1211 units per milligram protein and was purified 400-fold, with a yield of 8 micrograms enzyme per gram cotyledon. The glyoxysomal Cu,Zn-SOD had a relative molecular weight of about 33,000 and was composed of two equal subunits of 16,500 Daltons. Metal analysis showed that the enzyme, unlike other Cu,Zn-SODs, contained 1 gram-atom Cu and 1 gram-atom Zn per mole dimer. No iron and manganese were detected. Ultraviolet and visible absorption spectra were reminiscent of other copper,zinc-superoxide dismutases.

1 Supported by grant PB87-0404-01 from the Dirección General de Investigación Cientifica y Técnica (Spain).




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M. Rodriguez-Serrano, M. C. Romero-Puertas, G. M. Pastori, F. J. Corpas, L. M. Sandalio, L. A. del Rio, and J. M. Palma
Peroxisomal membrane manganese superoxide dismutase: characterization of the isozyme from watermelon (Citrullus lanatus Schrad.) cotyledons
J. Exp. Bot., July 1, 2007; 58(10): 2417 - 2427.
[Abstract] [Full Text] [PDF]


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Copyright © 1992 by the American Society of Plant Biologists