Purification and characterization of an abscisic acid-inducible anionic peroxidase associated with suberization in potato (Solanum tuberosum) |
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| Authors: | K E Espelie P E Kolattukudy |
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| Affiliation: | 1. “Alexandru Ioan Cuza” University of Iasi, Dept. Interdisciplinary Research- Field Science, Iasi, 700107, Romania;2. Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, Oxfordshire, United Kingdom;3. “Alexandru Ioan Cuza” University of Iasi, Faculty of Geography and Geology, Iasi, 700107, Romania;4. “Alexandru Ioan Cuza” University of Iasi, CERNESIM, Iasi, 700107, Romania;1. Institute of Plant Biology, National Taiwan University, Taipei, Taiwan;2. Hualien District Agricultural Research and Extension Station, Council of Agriculture, Hualien, Taiwan;3. AVRDC-The World Vegetable Center, PO Box 42, Shanhua, Tainan 74199, Taiwan;4. Ecological Materials Technology Department, Green Energy & Eco-technology System Center, ITRI South Campus, Industrial Technology Research Institute, Tainan, Taiwan;1. State Key Laboratory Cultivation Base for Nonmetal Composites and Functional Materials, Southwest University of Science and Technology, Mianyang 621010, China;2. College of Materials Science and Engineering, Sichuan University, Chengdu 610065, China;3. Department of Materials Science and Engineering, National Lab of Solid State Microstructure, ERERC, Nanjing University, Nanjing 210093, China |
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| Abstract: | An anionic peroxidase (EC 1.11.1.7), thought to be involved in suberization, was purified 110-fold from wound-healing slices of Solanum tuberosum by a combination of ammonium sulfate fractionation, Sephadex G-100 gel filtration, isoelectric focusing, and phenyl-Sepharose CL-4B chromatography in 24% yield. The purified enzyme was homogeneous as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and horizontal thin-layer polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be 47,000 by both Sephadex G-100 gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This peroxidase was found to be a glycoprotein containing about 17% carbohydrate, approximately one-quarter of which was shown to be glucosamine residues. It was found to have an isoelectric point of 3.15. An anionic peroxidase was also isolated from abscisic acid-treated callus tissue culture of S. tuberosum by the above purification procedure. The two enzymes were shown to be immunologically similar, if not identical, based on their cross-reactivity with rabbit antibody prepared against the peroxidase from wound-healing slices, whereas the major cationic peroxidase from wound-healing slices did not cross-react with this antibody. The anionic enzyme from both sources showed very similar specific activities when assayed with a range of substrates, whereas the specific activities found for the cationic isozyme isolated from wound-healing slices were quite different. |
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