Effect of H2O2 on tyrosine phosphorylation of pea proteins

Effect of H2O2 on tyrosine phosphorylation of pea proteins Changes in tyrosine phosphorylation of soluble polypeptides of pea (Pisum sativum L.) roots were revealed under the action of exogenous hydrogen peroxide in situ and in vitro. The polypeptides whose tyrosine phosphorylation in situ was vanadate-sensitive were identified. A thiol agent dithiothreitol and the antioxidant ascorbic acid reversed the effect of hydrogen peroxide in vitro. The results indicate that tyrosine phosphorylation of pea proteins is a subject to redox regulation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Effect of H2O2 on tyrosine phosphorylation of pea proteins

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Publisher
Nauka/Interperiodica
Copyright
Copyright © 2007 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Plant Physiology; Plant Sciences
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1134/S1021443707030053
Publisher site
See Article on Publisher Site

Abstract

Changes in tyrosine phosphorylation of soluble polypeptides of pea (Pisum sativum L.) roots were revealed under the action of exogenous hydrogen peroxide in situ and in vitro. The polypeptides whose tyrosine phosphorylation in situ was vanadate-sensitive were identified. A thiol agent dithiothreitol and the antioxidant ascorbic acid reversed the effect of hydrogen peroxide in vitro. The results indicate that tyrosine phosphorylation of pea proteins is a subject to redox regulation.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: May 25, 2007

References

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