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Peroxisomal Localization of CuZn Superoxide Dismutase in the Male Reproductive Tissues of the Olive Tree

Published online by Cambridge University Press:  28 September 2012

A. Zafra
Affiliation:
Department of Biochemistry, Cellular and Molecular Biology of Plants. Estación Experimental del Zaidín. CSIC. Granada, Spain
M. J. Jiménez-Quesada
Affiliation:
Department of Biochemistry, Cellular and Molecular Biology of Plants. Estación Experimental del Zaidín. CSIC. Granada, Spain
J. A. Traverso
Affiliation:
Department of Biochemistry, Cellular and Molecular Biology of Plants. Estación Experimental del Zaidín. CSIC. Granada, Spain
F. J. Corpas
Affiliation:
Department of Biochemistry, Cellular and Molecular Biology of Plants. Estación Experimental del Zaidín. CSIC. Granada, Spain
M. I. Rodríguez-García
Affiliation:
Department of Biochemistry, Cellular and Molecular Biology of Plants. Estación Experimental del Zaidín. CSIC. Granada, Spain
J. D. Alché
Affiliation:
Department of Biochemistry, Cellular and Molecular Biology of Plants. Estación Experimental del Zaidín. CSIC. Granada, Spain

Abstract

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Superoxide dismutases (SODs) are a class of antioxidant enzymes which catalyze the dismutation of superoxide into oxygen and hydrogen peroxide, therefore controlling cellular levels of Reactive Oxygen Species (ROS). In the mature pollen grains of the olive tree, the presence of several forms of CuZn-SOD and the cytosolic localization of the enzyme have been described. The present study was aimed to elucidate the adaptation of the oxidative metabolism to the changing conditions occurring during the course of olive pollen formation, hydration and pollen tube emergence and growth. We used a polyclonal antibody (raised against a KLH-linked synthetic peptide including a consensus sequence for CuZn-SODs in olive pollen) in immunocytochemical experiments carried out by Fluorescence (FM) and Transmission Electron Microcopy (TEM).

Type
Life Sciences
Copyright
Copyright © Microscopy Society of America 2012