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Glutathione reductase from pea leaves: response to abiotic stress and characterization of the peroxisomal isozyme.

Authors :
Romero-Puertas, María C.
Corpas, Francisco J.
Sandalio, Luisa M.
Leterrier, Marina
Rodríguez-Serrano, María
del Río, Luis A.
Palma, José M.
Source :
New Phytologist. Apr2006, Vol. 170 Issue 1, p43-52. 10p. 2 Charts, 4 Graphs.
Publication Year :
2006

Abstract

• The glutathione reductase (GR; EC 1.6.4.2) isozyme present in peroxisomes has been purified for the first time, and its unequivocal localization in these organelles, by immunogold electron microscopy, is reported. • The enzyme was purified c. 21-fold with a specific activity of 9523 units mg−1 protein, and a yield of 44 µg protein kg−1 leaves was obtained. The subunit size of the peroxisomal GR was 56 kDa and the isoelectric point was 5.4. The enzyme was recognized by a polyclonal antibody raised against total GR from pea ( Pisum sativum) leaves. • The localization of GR in peroxisomes adds to chloroplasts and mitochondria where GR isozymes are also present, and suggests a multiple targeting of this enzyme to distinct cell compartments depending on the metabolism of each organelle under the plant growth conditions. • The expression level of GR in several organs of pea plants and under different stress conditions was investigated. The possible role of peroxisomal GR under abiotic stress conditions, such as cadmium toxicity, high light, darkness, high temperature, wounding and low temperature, is discussed. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
0028646X
Volume :
170
Issue :
1
Database :
Academic Search Index
Journal :
New Phytologist
Publication Type :
Academic Journal
Accession number :
19901972
Full Text :
https://doi.org/10.1111/j.1469-8137.2006.01643.x