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Role of Apoplastic and Cell-Wall Peroxidases on the Stimulation of Root Elongation by Ascorbate.

Plant physiology

Cordoba-Pedregosa M, Gonzalez-Reyes JA, Canadillas M, Navas P, Cordoba F.
PMID: 12226436
Plant Physiol. 1996 Nov;112(3):1119-1125. doi: 10.1104/pp.112.3.1119.

Elongation of onion (Allium cepa L.) roots was highly stimulated by ascorbate (ASC) and its natural precursor I-galactone-[gamma]-lactone (GL). When incubation media were supplemented with lycorine (Lyc), an inhibitor of the ASC biosynthesis, root growth was negligible even in...

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Cordoba-Pedregosa M, Gonzalez-Reyes JA, Canadillas M, et al. Role of Apoplastic and Cell-Wall Peroxidases on the Stimulation of Root Elongation by Ascorbate. Plant Physiol. 1996;112(3):1119-1125doi: 10.1104/pp.112.3.1119.
Cordoba-Pedregosa, M., Gonzalez-Reyes, J. A., Canadillas, M., Navas, P., & Cordoba, F. (1996). Role of Apoplastic and Cell-Wall Peroxidases on the Stimulation of Root Elongation by Ascorbate. Plant physiology, 112(3), 1119-1125. https://doi.org/10.1104/pp.112.3.1119
Cordoba-Pedregosa, MdC., et al. "Role of Apoplastic and Cell-Wall Peroxidases on the Stimulation of Root Elongation by Ascorbate." Plant physiology vol. 112,3 (1996): 1119-1125. doi: https://doi.org/10.1104/pp.112.3.1119
Cordoba-Pedregosa M, Gonzalez-Reyes JA, Canadillas M, Navas P, Cordoba F. Role of Apoplastic and Cell-Wall Peroxidases on the Stimulation of Root Elongation by Ascorbate. Plant Physiol. 1996 Nov;112(3):1119-1125. doi: 10.1104/pp.112.3.1119. PMID: 12226436; PMCID: PMC158038.
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Abolition of an Inducible Highly Anionic Peroxidase Activity in Transgenic Tomato.

Plant physiology

Sherf BA, Bajar AM, Kolattukudy PE.
PMID: 12231677
Plant Physiol. 1993 Jan;101(1):201-208. doi: 10.1104/pp.101.1.201.

Locally induced expression of a highly anionic peroxidase has previously been correlated temporally and spatially with suberization of tissues responding to pathogen assault, wounding, or exogenously applied abscisic acid or fungal elicitors. DNA sequences corresponding to the 5[prime] regions...

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Sherf BA, Bajar AM, Kolattukudy PE. Abolition of an Inducible Highly Anionic Peroxidase Activity in Transgenic Tomato. Plant Physiol. 1993;101(1):201-208doi: 10.1104/pp.101.1.201.
Sherf, B. A., Bajar, A. M., & Kolattukudy, P. E. (1993). Abolition of an Inducible Highly Anionic Peroxidase Activity in Transgenic Tomato. Plant physiology, 101(1), 201-208. https://doi.org/10.1104/pp.101.1.201
Sherf, B. A., et al. "Abolition of an Inducible Highly Anionic Peroxidase Activity in Transgenic Tomato." Plant physiology vol. 101,1 (1993): 201-208. doi: https://doi.org/10.1104/pp.101.1.201
Sherf BA, Bajar AM, Kolattukudy PE. Abolition of an Inducible Highly Anionic Peroxidase Activity in Transgenic Tomato. Plant Physiol. 1993 Jan;101(1):201-208. doi: 10.1104/pp.101.1.201. PMID: 12231677; PMCID: PMC158665.
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Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases.

Plant physiology

Van Gestelen P, Asard H, Caubergs RJ.
PMID: 12223822
Plant Physiol. 1997 Oct;115(2):543-550. doi: 10.1104/pp.115.2.543.

Solubilization and ion-exchange chromatography of plasma membrane proteins obtained from bean (Phaseolus vulgaris L.) seedlings resulted in a single NAD(P)H-O2--synthase protein peak. This enzyme showed a high preference toward NADPH as a substrate (reaction rate, 27.4 nmol O2- produced...

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Van Gestelen P, Asard H, Caubergs RJ. Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant Physiol. 1997;115(2):543-550doi: 10.1104/pp.115.2.543.
Van Gestelen, P., Asard, H., & Caubergs, R. J. (1997). Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant physiology, 115(2), 543-550. https://doi.org/10.1104/pp.115.2.543
Van Gestelen, P., et al. "Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases." Plant physiology vol. 115,2 (1997): 543-550. doi: https://doi.org/10.1104/pp.115.2.543
Van Gestelen P, Asard H, Caubergs RJ. Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant Physiol. 1997 Oct;115(2):543-550. doi: 10.1104/pp.115.2.543. PMID: 12223822; PMCID: PMC158513.
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Biodegradation of superabsorbent polymers in soil.

Environmental science and pollution research international

Stahl JD, Cameron MD, Haselbach J, Aust SD.
PMID: 19009427
Environ Sci Pollut Res Int. 2000;7(2):83-8. doi: 10.1065/espr199912.014.

Biodegradation of two superabsorbent polymers, a crosslinked, insoluble polyacrylate and an insoluble polyacrylate/ polyacrylamide copolymer, in soil by the white-rot fungus, Phanerochaete chrysosporium was investigated. The polymers were both solubilized and mineralized by the fungus but solubilization and mineralization...

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Stahl JD, Cameron MD, Haselbach J, et al. Biodegradation of superabsorbent polymers in soil. Environ Sci Pollut Res Int. 2000;7(2):83-8doi: 10.1065/espr199912.014.
Stahl, J. D., Cameron, M. D., Haselbach, J., & Aust, S. D. (2000). Biodegradation of superabsorbent polymers in soil. Environmental science and pollution research international, 7(2), 83-8. https://doi.org/10.1065/espr199912.014
Stahl, J D, et al. "Biodegradation of superabsorbent polymers in soil." Environmental science and pollution research international vol. 7,2 (2000): 83-8. doi: https://doi.org/10.1065/espr199912.014
Stahl JD, Cameron MD, Haselbach J, Aust SD. Biodegradation of superabsorbent polymers in soil. Environ Sci Pollut Res Int. 2000;7(2):83-8. doi: 10.1065/espr199912.014. PMID: 19009427.
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Rapid Accumulation of Anionic Peroxidases and Phenolic Polymers in Soybean Cotyledon Tissues following Treatment with Phytophthora megasperma f. sp. Glycinea Wall Glucan.

Plant physiology

Graham MY, Graham TL.
PMID: 16668570
Plant Physiol. 1991 Dec;97(4):1445-55. doi: 10.1104/pp.97.4.1445.

Phytophthora megasperma Drechs. f. sp. glycinea Kuan & Erwin (PMG) cell wall glucan has been extensively characterized as an elicitor of the pterocarpan phytoalexins, the glyceollins in soybean (Glycine max L.). Just recently, this glucan was shown to be...

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Graham MY, Graham TL. Rapid Accumulation of Anionic Peroxidases and Phenolic Polymers in Soybean Cotyledon Tissues following Treatment with Phytophthora megasperma f. sp. Glycinea Wall Glucan. Plant Physiol. 1991;97(4):1445-55doi: 10.1104/pp.97.4.1445.
Graham, M. Y., & Graham, T. L. (1991). Rapid Accumulation of Anionic Peroxidases and Phenolic Polymers in Soybean Cotyledon Tissues following Treatment with Phytophthora megasperma f. sp. Glycinea Wall Glucan. Plant physiology, 97(4), 1445-55. https://doi.org/10.1104/pp.97.4.1445
Graham, M Y, and Graham, T L. "Rapid Accumulation of Anionic Peroxidases and Phenolic Polymers in Soybean Cotyledon Tissues following Treatment with Phytophthora megasperma f. sp. Glycinea Wall Glucan." Plant physiology vol. 97,4 (1991): 1445-55. doi: https://doi.org/10.1104/pp.97.4.1445
Graham MY, Graham TL. Rapid Accumulation of Anionic Peroxidases and Phenolic Polymers in Soybean Cotyledon Tissues following Treatment with Phytophthora megasperma f. sp. Glycinea Wall Glucan. Plant Physiol. 1991 Dec;97(4):1445-55. doi: 10.1104/pp.97.4.1445. PMID: 16668570; PMCID: PMC1081185.
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The Effect of Pseudomonas putida Colonization on Root Surface Peroxidase.

Plant physiology

Albert F, Anderson AJ.
PMID: 16665732
Plant Physiol. 1987 Oct;85(2):537-41. doi: 10.1104/pp.85.2.537.

Increased activities of peroxidase and indole 3-acetic acid (IAA) oxidase were detected on root surfaces of bean (Phaseolus vulgaris) seedlings colonized with a soil saprophytic bacterium, Pseudomonas putida. IAA oxidase activity increased over 250-fold and peroxidase 8-fold. Enhancement was...

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Albert F, Anderson AJ. The Effect of Pseudomonas putida Colonization on Root Surface Peroxidase. Plant Physiol. 1987;85(2):537-41doi: 10.1104/pp.85.2.537.
Albert, F., & Anderson, A. J. (1987). The Effect of Pseudomonas putida Colonization on Root Surface Peroxidase. Plant physiology, 85(2), 537-41. https://doi.org/10.1104/pp.85.2.537
Albert, F, and Anderson, A J. "The Effect of Pseudomonas putida Colonization on Root Surface Peroxidase." Plant physiology vol. 85,2 (1987): 537-41. doi: https://doi.org/10.1104/pp.85.2.537
Albert F, Anderson AJ. The Effect of Pseudomonas putida Colonization on Root Surface Peroxidase. Plant Physiol. 1987 Oct;85(2):537-41. doi: 10.1104/pp.85.2.537. PMID: 16665732; PMCID: PMC1054290.
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Purification and Characterization of Isoperoxidases Elicited by Aspergillus flavus in Cotton Ovule Cultures.

Plant physiology

Mellon JE.
PMID: 16667941
Plant Physiol. 1991 Jan;95(1):14-20. doi: 10.1104/pp.95.1.14.

Two anionic isoperoxidases were isolated from media of Aspergillus flavus-inoculated cotton (Gossypium hirsutum L.) ovule cultures and purified about 150-fold to apparent homogeneity by treatment with Cell Debris Remover and ion exchange chromatography on Accell QMA medium. These isoperoxidases...

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Mellon JE. Purification and Characterization of Isoperoxidases Elicited by Aspergillus flavus in Cotton Ovule Cultures. Plant Physiol. 1991;95(1):14-20doi: 10.1104/pp.95.1.14.
Mellon, J. E. (1991). Purification and Characterization of Isoperoxidases Elicited by Aspergillus flavus in Cotton Ovule Cultures. Plant physiology, 95(1), 14-20. https://doi.org/10.1104/pp.95.1.14
Mellon, J E. "Purification and Characterization of Isoperoxidases Elicited by Aspergillus flavus in Cotton Ovule Cultures." Plant physiology vol. 95,1 (1991): 14-20. doi: https://doi.org/10.1104/pp.95.1.14
Mellon JE. Purification and Characterization of Isoperoxidases Elicited by Aspergillus flavus in Cotton Ovule Cultures. Plant Physiol. 1991 Jan;95(1):14-20. doi: 10.1104/pp.95.1.14. PMID: 16667941; PMCID: PMC1077478.
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Peroxidases in Tobacco Abscission Zone Tissue: II. Time Course Studies of Peroxidase Activity during Ethylene-induced Abscission.

Plant physiology

Henry EW, Valdovinos JG, Jensen TE.
PMID: 16658858
Plant Physiol. 1974 Aug;54(2):192-6. doi: 10.1104/pp.54.2.192.

Ethylene-induced abscission in flower pedicels of Nicotiana tabacum L. cv. Little Turkish causes a progressive increase in peroxidase activity during the first 4 hours of a 5-hour time course ethylene treatment period, with decrease in peroxidase activity occurring between...

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Henry EW, Valdovinos JG, Jensen TE. Peroxidases in Tobacco Abscission Zone Tissue: II. Time Course Studies of Peroxidase Activity during Ethylene-induced Abscission. Plant Physiol. 1974;54(2):192-6doi: 10.1104/pp.54.2.192.
Henry, E. W., Valdovinos, J. G., & Jensen, T. E. (1974). Peroxidases in Tobacco Abscission Zone Tissue: II. Time Course Studies of Peroxidase Activity during Ethylene-induced Abscission. Plant physiology, 54(2), 192-6. https://doi.org/10.1104/pp.54.2.192
Henry, E W, et al. "Peroxidases in Tobacco Abscission Zone Tissue: II. Time Course Studies of Peroxidase Activity during Ethylene-induced Abscission." Plant physiology vol. 54,2 (1974): 192-6. doi: https://doi.org/10.1104/pp.54.2.192
Henry EW, Valdovinos JG, Jensen TE. Peroxidases in Tobacco Abscission Zone Tissue: II. Time Course Studies of Peroxidase Activity during Ethylene-induced Abscission. Plant Physiol. 1974 Aug;54(2):192-6. doi: 10.1104/pp.54.2.192. PMID: 16658858; PMCID: PMC541529.
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Soluble and cell wall peroxidases in reed canarygrass in relation to disease resistance and localized lignin formation.

Plant physiology

Vance CP, Anderson JO, Sherwood RT.
PMID: 16659599
Plant Physiol. 1976 Jun;57(6):920-2. doi: 10.1104/pp.57.6.920.

The relationship of peroxidases to an inducible disease-resistance mechanism involving lignification of leaf epidermal cell walls was studied. Reed canarygrass (Phalaris arundinacea L.) leaf discs were inoculated with Helminthosporium avenae Eidam and floated on water. In inoculated discs, the...

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Vance CP, Anderson JO, Sherwood RT. Soluble and cell wall peroxidases in reed canarygrass in relation to disease resistance and localized lignin formation. Plant Physiol. 1976;57(6):920-2doi: 10.1104/pp.57.6.920.
Vance, C. P., Anderson, J. O., & Sherwood, R. T. (1976). Soluble and cell wall peroxidases in reed canarygrass in relation to disease resistance and localized lignin formation. Plant physiology, 57(6), 920-2. https://doi.org/10.1104/pp.57.6.920
Vance, C P, et al. "Soluble and cell wall peroxidases in reed canarygrass in relation to disease resistance and localized lignin formation." Plant physiology vol. 57,6 (1976): 920-2. doi: https://doi.org/10.1104/pp.57.6.920
Vance CP, Anderson JO, Sherwood RT. Soluble and cell wall peroxidases in reed canarygrass in relation to disease resistance and localized lignin formation. Plant Physiol. 1976 Jun;57(6):920-2. doi: 10.1104/pp.57.6.920. PMID: 16659599; PMCID: PMC542149.
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Peroxidase Release Induced by Ozone in Sedum album Leaves: Involvement of Ca.

Plant physiology

Castillo FJ, Penel C, Greppin H.
PMID: 16663520
Plant Physiol. 1984 Apr;74(4):846-51. doi: 10.1104/pp.74.4.846.

The effect of ozone was studied on the peroxidase activity from various compartments of Sedum album leaves (epidermis, intercellular fluid, residual cell material, and total cell material). The greatest increase following a 2-hour ozone exposure (0.4 microliters O(3) per...

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Castillo FJ, Penel C, Greppin H. Peroxidase Release Induced by Ozone in Sedum album Leaves: Involvement of Ca. Plant Physiol. 1984;74(4):846-51doi: 10.1104/pp.74.4.846.
Castillo, F. J., Penel, C., & Greppin, H. (1984). Peroxidase Release Induced by Ozone in Sedum album Leaves: Involvement of Ca. Plant physiology, 74(4), 846-51. https://doi.org/10.1104/pp.74.4.846
Castillo, F J, et al. "Peroxidase Release Induced by Ozone in Sedum album Leaves: Involvement of Ca." Plant physiology vol. 74,4 (1984): 846-51. doi: https://doi.org/10.1104/pp.74.4.846
Castillo FJ, Penel C, Greppin H. Peroxidase Release Induced by Ozone in Sedum album Leaves: Involvement of Ca. Plant Physiol. 1984 Apr;74(4):846-51. doi: 10.1104/pp.74.4.846. PMID: 16663520; PMCID: PMC1066779.
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Characterization of peroxidase in plant cells.

Plant physiology

Chibbar RN, van Huystee RB.
PMID: 16663767
Plant Physiol. 1984 Aug;75(4):956-8. doi: 10.1104/pp.75.4.956.

Two peroxidases, one anionic and one cationic, have been purified from the proteins secreted by peanut (Arachis hypogaea L. var Virginia 56R) cells in suspension culture. These two peroxidases apparently have identical catalytic properties.

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Chibbar RN, van Huystee RB. Characterization of peroxidase in plant cells. Plant Physiol. 1984;75(4):956-8doi: 10.1104/pp.75.4.956.
Chibbar, R. N., & van Huystee, R. B. (1984). Characterization of peroxidase in plant cells. Plant physiology, 75(4), 956-8. https://doi.org/10.1104/pp.75.4.956
Chibbar, R N, and van Huystee, R B. "Characterization of peroxidase in plant cells." Plant physiology vol. 75,4 (1984): 956-8. doi: https://doi.org/10.1104/pp.75.4.956
Chibbar RN, van Huystee RB. Characterization of peroxidase in plant cells. Plant Physiol. 1984 Aug;75(4):956-8. doi: 10.1104/pp.75.4.956. PMID: 16663767; PMCID: PMC1067031.
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Production and Preliminary Characterization of Monoclonal Antibodies against Cationic Peanut Peroxidase.

Plant physiology

Hu C, Carbonera D, van Huystee R.
PMID: 16665674
Plant Physiol. 1987 Sep;85(1):299-303. doi: 10.1104/pp.85.1.299.

Ten monoclonal antibodies (McAbs) have been produced against the cationic peroxidase from peanut suspension cell culture. Eight of these antibodies were found to be of the immunoglobulin (Ig)G(1) subclass and two were of IgA subclass. A combination of competitive...

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Hu C, Carbonera D, van Huystee R. Production and Preliminary Characterization of Monoclonal Antibodies against Cationic Peanut Peroxidase. Plant Physiol. 1987;85(1):299-303doi: 10.1104/pp.85.1.299.
Hu, C., Carbonera, D., & van Huystee, R. (1987). Production and Preliminary Characterization of Monoclonal Antibodies against Cationic Peanut Peroxidase. Plant physiology, 85(1), 299-303. https://doi.org/10.1104/pp.85.1.299
Hu, C, et al. "Production and Preliminary Characterization of Monoclonal Antibodies against Cationic Peanut Peroxidase." Plant physiology vol. 85,1 (1987): 299-303. doi: https://doi.org/10.1104/pp.85.1.299
Hu C, Carbonera D, van Huystee R. Production and Preliminary Characterization of Monoclonal Antibodies against Cationic Peanut Peroxidase. Plant Physiol. 1987 Sep;85(1):299-303. doi: 10.1104/pp.85.1.299. PMID: 16665674; PMCID: PMC1054245.
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Showing 25 to 36 of 590 entries