Plant and Cell Physiology Supplement
Supplement to Plant and Cell Physiology Vol. 47
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Proteome analysis of poplar peroxidase isoenzymes
*Shinya SasakiMotoyuki ShimizuHiroyuki WariishiYuji TsutsumiRyuichirou Kondo
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Pages 463

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Abstract
Higher plants possess a large set of the class III plant peroxidases. These peroxidases are thought to participate in a wide rage of physiological functions, however, the most of their functions have been unclear. Using proteomic analysis, we surveyed the localization of plant peroxidase in various organs in Populus alba. Peroxidase isoenzymes were extracted from the various organs and fractionated by a Concanavallin A Sepharose column. Each peroxidase protein was identified by the Peptide Mass Fingerprint analysis. All organs expressed anionic peroxidase isoenzymes dominantly, and they are composed in a small cluster of phylogenic tree of poplar peroxidases. Interestingly, each organ has different peroxidase constitution. These results suggest that individual peroxidase isoenzyme in this cluster is regulated under different transcriptional or translational control.
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© 2006 by The Japanese Society of Plant Physiologists
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