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JXB Advance Access originally published online on June 1, 2007
Journal of Experimental Botany 2007 58(10):2417-2427; doi:10.1093/jxb/erm095
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© 2007 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

Peroxisomal membrane manganese superoxide dismutase: characterization of the isozyme from watermelon (Citrullus lanatus Schrad.) cotyledons

María Rodríguez-Serrano, María C. Romero-Puertas *, Gabriela M. Pastori {dagger}, Francisco J. Corpas, Luisa M. Sandalio, Luis A. del Río and José M. Palma{ddagger}

Departamento de Bioquímica, Biología Celular y Molecular de Plantas, Estación Experimental del Zaidín, CSIC, Apartado 419, E-18080 Granada, Spain

{ddagger} To whom correspondence should be addressed. E-mail: jmpalma{at}eez.csic.es

In this work the manganese superoxide dismutase (Mn-SOD) bound to peroxisomal membranes of watermelon cotyledons (Citrullus lanatus Schrad.) was purified to homogeneity and some of its molecular properties were determined. The stepwise purification procedure consisted of ammonium sulphate fractionation, batch anion-exchange chromatography, and anion-exchange and gel-filtration column chromatography using a fast protein liquid chromatography system. Peroxisomal membrane Mn-SOD (perMn-SOD; EC 1.15.1.1) was purified 5600-fold with a yield of 2.6 µg of enzyme g–1 of cotyledons, and had a specific activity of 480 U mg–1 of protein. The native molecular mass determined for perMn-SOD was 108 000 Da, and it was composed of four equal subunits of 27 kDa, which indicates that perMn-SOD is a homotetramer. Ultraviolet and visible absorption spectra of the enzyme showed a shoulder at 275 nm and two absorption maxima at 448 nm and 555 nm, respectively. By isoelectric focusing, a pI of 5.75 was determined for perMn-SOD. In immunoblot assays, purified perMn-SOD was recognized by a polyclonal antibody against Mn-SOD from pea leaves, and the peroxisomal enzyme rapidly dissociated in the presence of dithiothreitol and SDS. The potential binding of the Mn-SOD isozyme to the peroxisomal membrane was confirmed by immunoelectron microscopy analysis. The properties of perMn-SOD and the mitMn-SOD are compared and the possible function in peroxisomal membranes of the peripheral protein Mn-SOD is discussed.

Key words: Germination, glyoxysomes, manganese superoxide dismutase, mitochondria, peroxisomes, watermelon (Citrullus lanatus), western blotting

* Present address: Disease and Stress Biology Department, John Innes Centre, Norwich Research Park, Colney Lane, Norwich NR4 7UH, UK.

{dagger} Present address: Crop Performance and Improvement Division, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, UK.

Received 2 November 2006; Revised 12 April 2007 Accepted 17 April 2007


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