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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Superoxide dismutase: An enzyme system for the study of micronutrient interactions in plants
L A Del Río1, F Sevilla, M Gómez
1Sección de Bioquímica, Estación Experimental del Zaidín, C.S.I.C., Profesor Albareda 1, Granada, Spain.
Abstract:
The effect of different Mn levels on the isozyme pattern of superoxide dismutase was investigated. Pisum sativum L. plants were grown in nutrient solutions containing three Mn concentrations: 0.005 μg/ml (deficient), 0.05 μg/ml (low), and 0.5 μg/ml (optimum). Leaf extracts contained three electrophoretically distinct superoxide dismutases (SOD), two of which were inhibited by cyanide and were probably Cu-Zn-SODs, while the third one was CN-insensitive and could be either an Mn- or an Fe-SOD. At 0.005 μg/ml Mn supply the CN-insensitive SOD was significantly depressed at 15, 30, and 45 days of growth, whereas at 0.05 μg/ml Mn this isozyme was significantly decreased only at 45 days growth. The two CN-sensitive SODs were inversely related to the CN-resistant enzyme, the activities of the former enzymes being significantly increased at Mn-deficient levels throughout plant growth. Metal determinations of the plants showed that at low concentrations of Mn in the nutrient media, copper and zinc content of leaves increased: the lower the Mn level, the higher the increase produced. The CN-resistant SOD activity, as judged by its dependency on Mn, appears to be an Mn-SOD rather than an Fe-SOD. In the light of the results obtained, the use of the enzyme system superoxide dismutase for the study of the role and interactions between Mn, Cu, and Zn in the plant cell is proposed.
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