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PLANT PHYSIOLOGY , Vol 108, Issue 3 1151-1160, Copyright © 1995 by American Society of Plant Biologists

BIOCHEMISTRY AND ENZYMOLOGY

Peroxisomal Copper,Zinc Superoxide Dismutase (Characterization of the Isoenzyme from Watermelon Cotyledons)

P. Bueno, J. Varela, G. Gimenez-Gallego and L. A. del Rio
Departamento de Bioquimica, Biologia Celular y Molecular de Plantas, Estacion Experimental del Zaidin, Consejo Superior de Investigaciones Cientificas, Granada, Spain (P.B., L.A.d.R.)

The biochemical and immunochemical characterization of a superoxide dismutase (SOD, EC 1.15.1.1) from peroxisomal origin has been carried out. The enzyme is a Cu,Zn-containing SOD (CuZn-SOD) located in the matrix of peroxisomes from watermelon (Citrullus vulgaris Schrad.) cotyledons (L.M. Sandalio and L.A. del Rio [1988] Plant Physiol 88: 1215-1218). The amino acid composition of the enzyme was determined. Analysis by reversed-phase high-performance liquid chromatography of the peroxisomal CuZn-SOD incubated with 6 M guanidine-HCI indicated that this enzyme contained a noncovalently bound chromophore group that was responsible for the absorbance peak of the native enzyme at 260 nm. The amino acid sequence of the peroxisomal CuZn-SOD was determined by Edman degradation. Comparison of its sequence with those reported for other plant SODs revealed homologies of about 70% with cytosolic CuZn-SODs and of 90% with chloroplastic CuZn-SODs. The peroxisomal SOD has a high thermal stability and resistance to inactivation by hydrogen peroxide. A polyclonal antibody was raised against peroxisomal CuZn-SOD, and by western blotting the antibody cross-reacted with plant CuZn-SODs but did not recognize either plant Mn-SOD or bacterial Fe-SOD. The antiSOD-immunoglobulin G showed a weak cross-reaction with bovine erythrocytes and liver CuZn-SODs, and also with cell-free extracts from trout liver. The possible function of this CuZn-SOD in the oxidative metabolism of peroxisomes is discussed.


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Copyright © 1995 by the American Society of Plant Biologists