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Superoxide Dismutase Activity in Needles of Norwegian Spruce Trees (Picea abies L.)

Superoxide Dismutase Activity in Needles of Norwegian Spruce Trees (Picea abies L.) Abstract The activity of superoxide dismutase was investigated in needles of spruce trees. To obtain maximum activity, needles were homogenized in the presence of Triton X-100 and polyvinylpyrrolidone. Superoxide dismutase activity was measured in dialyzed extracts with a modified epinephrine assay (HP Misra, I Fridovich [1972] J Biol Chem 247: 3170-3175) at pH 10.2. The extracts contained 70 to 120 units of superoxide dismutase per milligram protein. One unit of superoxide dismutase was completely inhibited in the presence of 20 micromolar NaCN. On native polyacrylamide gels three electromorphs were visualized after staining for activity. All three species were sensitive to CN− and H2O2 and were therefore assumed to be Cu/Zn-superoxide dismutases. Superoxide dismutase activity was dependent on the age of the needles and declined by approximately 25% within 3 to 4 years. 1 This work was financially supported by the Bundesminister für Forschung and Technologie under contract No. 0339019B7. This content is only available as a PDF. © 1989 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model) http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Physiology Oxford University Press

Superoxide Dismutase Activity in Needles of Norwegian Spruce Trees (Picea abies L.)

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References (25)

Publisher
Oxford University Press
Copyright
Copyright © 2021 American Society of Plant Biologists
ISSN
0032-0889
eISSN
1532-2548
DOI
10.1104/pp.90.4.1310
Publisher site
See Article on Publisher Site

Abstract

Abstract The activity of superoxide dismutase was investigated in needles of spruce trees. To obtain maximum activity, needles were homogenized in the presence of Triton X-100 and polyvinylpyrrolidone. Superoxide dismutase activity was measured in dialyzed extracts with a modified epinephrine assay (HP Misra, I Fridovich [1972] J Biol Chem 247: 3170-3175) at pH 10.2. The extracts contained 70 to 120 units of superoxide dismutase per milligram protein. One unit of superoxide dismutase was completely inhibited in the presence of 20 micromolar NaCN. On native polyacrylamide gels three electromorphs were visualized after staining for activity. All three species were sensitive to CN− and H2O2 and were therefore assumed to be Cu/Zn-superoxide dismutases. Superoxide dismutase activity was dependent on the age of the needles and declined by approximately 25% within 3 to 4 years. 1 This work was financially supported by the Bundesminister für Forschung and Technologie under contract No. 0339019B7. This content is only available as a PDF. © 1989 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Journal

Plant Physiology – Oxford University Press

Published: Aug 1, 1989

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