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  • 11
    Online Resource
    Online Resource
    Nitric Oxide and Hydrogen Peroxide Signaling in Higher Plants (2019)
    Cham : Springer
    Details Availability
    Keywords: Biochemistry ; Plant diseases ; Cytology ; Plant Physiology ; Plant physiology ; Plant anatomy ; Plant biochemistry. ; Plant development. ; Plant pathology. ; Oxidative stress.
    Description / Table of Contents: Chapter 1. Hydrogen peroxide and nitric oxide generation in plant cells: Overview and queries -- Chapter 2.Nitric oxide and hydrogen peroxide signalling network -- Chapter 3.H2O2 and NO derived posttranslational modifications -- Chapter 4.Transcriptional regulation of gene expression related to NO and H2O2.-Chapter 5.Metabolism and interplay of reactive oxygen and nitrogen species in plant mitochondria -- Chapter 6.Hydrogen peroxide and nitric oxide metabolism in chloroplasts -- Chapter 7.Participation of nitric oxide and hydrogen peroxide in regulation of seed germination -- Chapter 8.Nitric oxide and hydrogen peroxide in root organogenesis -- Chapter 9.Nitric oxide and Hydrogen peroxide: signals in fruit ripening -- Chapter 10.Plant abiotic stress: function of Nitric oxide and Hydrogen peroxide -- Chapter 11.Nitric oxide and Hydrogen peroxide in plant response to biotic stress -- Chapter 12.Biotechnological application of Nitric oxide and Hydrogen peroxide in plants
    Type of Medium: Online Resource
    Pages: 1 Online-Ressource (XI, 270 p. 24 illus., 23 illus. in color)
    ISBN: 9783030111298
    Series Statement: Springer eBooks
    URL: https://doi.org/10.1007/978-3-030-11129-8
    DOI: 10.1007/978-3-030-11129-8
    Language: English
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  • 12
    Online Resource
    Online Resource
    Antioxidants and Antioxidant Enzymes in Higher Plants (2018)
    Cham : Springer International Publishing
    Details Availability
    Keywords: Life sciences ; Life Sciences ; Plant biochemistry ; Oxidative stress ; Plant physiology ; Life sciences ; Plant biochemistry ; Oxidative stress ; Plant physiology ; Kormophyten ; Antioxidans ; Enzym ; Kormophyten ; Antioxidans ; Enzym
    Description / Table of Contents: Plant superoxide dismutases: Function under abiotic stress conditions -- Studies of catalase in plants under abiotic stress -- Ascorbate peroxidase functions in higher plants: The control of the balance between oxidative damage and signaling -- Glutathione reductase: Safeguarding plant cells against oxidant damage -- Function of the various MDAR isoforms in higher plants -- Peroxiredoxins: Types, characteristics and functions in higher plants -- Redox protein thioredoxins: Function under salinity, drought and extreme temperature conditions -- Biosynthesis and regulation of ascorbic acid in plants -- Glutathione metabolism and its function in higher plants adapting to stress -- Revisiting carotenoids and their role in plant stress responses: From biosynthesis to plant signaling mechanisms during stress. Abiotic stress response in plants – the relevance of tocopherols -- Role of flavonoids in plant stress. Class III peroxidases: isoenzymes functions, localization and redox regulation.
    Type of Medium: Online Resource
    Pages: Online-Ressource (XIII, 300 p. 30 illus., 22 illus. in color, online resource)
    ISBN: 9783319750880
    Series Statement: SpringerLink
    URL: https://doi.org/10.1007/978-3-319-75088-0
    URL: http://dx.doi.org/10.1007/978-3-319-75088-0
    URL: https://swbplus.bsz-bw.de/bsz497195976cov.jpg
    DOI: 10.1007/978-3-319-75088-0
    RVK:
    WD 5055
    RVK:
    WN 1950
    Language: English
    Note: Includes bibliographical references
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  • 13
    Online Resource
    Online Resource
    Melatonin: Role in Plant Signaling, Growth and Stress Tolerance : Phytomelatonin in normal and challenging environments (2023)
    Cham : Springer International Publishing | Cham : Imprint: Springer
    Details Availability
    Keywords: Botany. ; Plants. ; Botanical chemistry. ; Stress (Physiology).
    Description / Table of Contents: Preface -- I. Melatonin as an antioxidant -- Chapter 1. Melatonin and the metabolism of reactive oxygen species (ROS) in higher plants -- II. Melatonin, biosynthesis, plant growth, development and reproduction -- Chapter 2. Melatonin in Plants: Biosynthesis, Occurrence and Role in plants -- Chapter 3. Abiotic stress-induced modulation of melatonin biosynthesis accompanying phytohormonal crosstalk in plants -- Chapter 4. Role of melatonin in embryo, seed development and germination -- Chapter 5. Melatonin metabolism in seeds: physiological and nutritive aspects -- Chapter 6. Melatonin in plant growth and signaling -- Chapter 7. Functions and prospects of melatonin during pre-fertilization reproductive stages in plants -- Chapter 8. Melatonin and fruit ripening physiology: crosstalk with ethylene, nitric oxide, hydrogen peroxide and hydrogen sulfide -- Chapter 9. Melatonin and postharvest biology of fruits and vegetables: augmenting the endogenous molecule by exogenous application -- Chapter 10. Melatonin language in postharvest life of horticultural crops -- III. Melatonin and its signaling in biotic and abiotic stress -- Chapter 11. Melatonin-mediated regulation of biotic stress responses in plants -- Chapter 12. Emerging roles of melatonin in mitigating pathogen stress -- Chapter 13. Eco-physiological and morphological adaptive mechanisms induced by melatonin and hydrogen sulfide under abiotic stresses in plants -- Chapter 14. Melatonin in plants under UV stress conditions -- Chapter 15. Molecular physiology of melatonin induced temperature stress tolerance in plants -- Chapter 16. Melatonin-mediated salt tolerance in plants -- Chapter 17. Role of phytomelatonin in promoting ion homeostasis during salt stress -- Chapter 18. Positive regulatory role of melatonin in conferring drought resistance to plants -- Chapter 19. Potential, mechanism and molecular insight of melatonin in phytoremediation.
    Type of Medium: Online Resource
    Pages: 1 Online-Ressource(IX, 386 p. 1 illus.)
    Edition: 1st ed. 2023.
    ISBN: 9783031401732
    Series Statement: Plant in Challenging Environments 4
    URL: https://doi.org/10.1007/978-3-031-40173-2
    DOI: 10.1007/978-3-031-40173-2
    Language: English
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  • 14
    Electronic Resource
    Electronic Resource
    Salt-induced oxidative stress mediated by activated oxygen species in pea leaf mitochondria (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 89 (1993), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effect in vivo of salt stress on the activated oxygen metabolism of mitochondria, was studied in leaves from two NaCl-treated cultivars of Pisum sativum L. with different sensitivity to NaCl. In mitochondria from NaCl-sensitive plants, salinity brought about a significant decrease of Mn-SOD (EC 1. 15. 1. 1) Cu, Zn-SOD I (EC 1. 15. 1. 1) and fumarase (EC 4. 2. 1. 2) activities. Conversely, in salt-tolerant plants NaCl treatment produced an increase in the mitochondrial Mn-SOD activity and, to a lesser extent, in fumarase activity. In mitochondria from both salt-treated cultivars, the internal H2O2 concentration remained unchanged. The NADH- and succinate-dependent generation of O2.−radicals by submitochondrial particles and the lipid peroxidation of mitochondrial membranes, increased as a result of salt treatment, and these changes were higher in NaCl-sensitive than in NaCl-tolerant plants. Accordingly, the enhanced rates of superoxide production by mitochondria from salt-sensitive plants were concomitant with a strong decrease in the mitochondrial Mn-SOD activity, whereas NaCl-tolerant plants appear to have a protection mechanism against salt-induced increased O2.− production by means of the induction of the mitochondrial Mn-SOD activity. These results indicate that in the subcellular toxicity of NaCl in pea plants, at the level of mitochondria, an oxidative stress mechanism mediated by superoxide radicals is involved, and also imply a function for mitochondrial Mn-SOD in the molecular mechanisms of plant tolerance to NaCl.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1993.tb01792.x
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  • 15
    Electronic Resource
    Electronic Resource
    Activated oxygen-mediated metabolic functions of leaf peroxisomes (1998)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Peroxisomes are subcellular organelles with an essentially oxidative type of metabolism. The presence in these organelles of superoxide dismutases and the generation of superoxide radicals (O2•−) was first demonstrated in plant tissues and in recent years different experimental evidence has suggested the existence of cellular functions related to activated oxygen species. Some of these functions are analyzed in this work.In purified intact peroxisomes from pea (Pisum sativum L.) leaves, xanthine oxidase and urate oxidase were found to be present. The occurrence and the level of the metabolites xanthine, hypoxanthine, uric acid, and allantoin were studied in extracts of pea leaf peroxisomes by HPLC. Xanthine, uric acid, and allantoin were detected in peroxisomes. These results suggest a cellular role for leaf peroxisomes in the catabolism of purines.In peroxisomal membranes, 3 polypeptides (PMPs) with molecular masses of 18, 29 and 32 kDa, respectively, have been shown to generate superoxide radicals. These PMPs were purified from pea leaf peroxisomal membranes and characterized. While the 18- and 32-kDa PMPs use NADH as electron donor for O2•− production, the 29-kDa PMP was clearly dependent on NADPH.Very recently, the occurrence in pea leaf peroxisomes of all the enzymes of the ascorbate-glutathione cycle has been demonstrated. NADPH is required for the glutathione reductase activity of the cycle and this implies the reduction of NADP+ to NADPH. This recycling function could be carried out by the NADP-dependent glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH), and isocitrate dehydrogenase (ICDH). These 3 dehydrogenases have been demonstrated to be present in the matrix of pea leaf peroxisomes.The catabolism of purines, the superoxide-generating PMPs, the ascorbate-glutathione cycle, and the dehydrogenase-mediated recycling of NADPH, are activated oxygen roles of leaf peroxisomes that add to other functions previously known for peroxisomes from eukaryotic cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1998.1040422.x
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  • 16
    Electronic Resource
    Electronic Resource
    Peroxisomal manganese superoxide dismutase: Purification and properties of the isozyme from pea leaves (1998)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The peroxisomal manganese superoxide dismutase (perMn-SOD; EC 1.15.1.1) was purified to homogeneity for the first time from peroxisomes of pea (Pisum sativum L.) leaves. Peroxisomes were isolated from pea leaves by sucrose density-gradient centrifugation, and then perMn-SOD was purified from these organelles by two purification steps involving anion-exchange and gel-filtration fast protein liquid chromatography. Pure peroxisomal Mn-SOD had a specific activity of 2 880 units per mg protein and was purified 3 000-fold, with a yield of about 7 µg enzyme per kg pea leaves. The relative molecular mass determined for perMn-SOD was 92 000, and it was composed of four equal subunits of 27 kDa. Ultraviolet and visible absorption spectra of the enzyme showed two absorption maxima at 278 and 483 nm, respectively, and two shoulders at 290 and 542 nm. By isoelectric focusing (pH 5-7), an isoelectric point of 5.53 was determined for perMn-SOD. In immunoblot assays, purified Mn-SOD was recognized by a polyclonal antibody against mitochondrial Mn-SOD (mitMn-SOD) from pea leaves. The amino acid sequence of the N-terminal region of the purified peroxisomal enzyme was determined. A 100% identity was found with the mitMn-SOD from pea leaves, and high identities were also found with Mn-SODs from other plant species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1998.1040429.x
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  • 17
    Electronic Resource
    Electronic Resource
    Identification and immunolocalization of superoxide dismutase isoenzymes of olive pollen (1998)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Gametophytic tissues of plants are an area largely neglected in the broad literature on free radical processes in plants. In order to study the mechanisms of protection against oxidative stress in pollen, the presence of the key antioxidative enzyme superoxide dismutase (SOD; EC 1.15.1.1) was investigated. Crude extracts of olive tree (Olea europaea L.) pollen were subjected to native PAGE in 10% polyacrylamide gels. The SOD activity staining of gels showed the presence of four isoenzymes. All the SODS were completely inhibited by 2 mM KCN and 5 mM H2O2, and therefore belong to the family of CuZn-SODS. Isoelectric focusing (pH 3.5-7) of crude extracts and further detection of SOD activity allowed determination of isoelectric points for the four isoforms, namely 4.60, 4.78, 5.08 and 5.22. The cross-reactivity of pollen extracts with a polyclonal antibody to cytosolic CuZn-SOD from spinach leaves was assayed by western blotting. After SDS-PAGE and immunoblotting, a major polypeptide band of about 16.5 kDa was detected, which is characteristic of the subunit of most CuZn-SODS. Immunocytochemical studies at TEM level using the same antiserum showed that CuZn-SOD was localized in the cytoplasm of both vegetative and generative cells, and also in material adhered to the pollen wall. The olive pollen CuZn-SODS could function in the protection against oxidative stress during pollen development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1998.1040437.x
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  • 18
    Electronic Resource
    Electronic Resource
    Subcellular distribution of superoxide dismutase in leaves of ureide-producing leguminous plants (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 82 (1991), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The subcellular localization of superoxide dismutase (SOD; EC. 1.15.1.1) was studied in leaves of two ureide-producing leguminous plants (Phaseolus vulgaris L. cv. Contender and Vigna unguiculata [L.] Walp). In leaves of Vigna and Phaseolus, three superoxide dismutases were found, an Mn-SOD and two Cu, Zn-containing SODs (I and II). Chloroplasts, mitochondria, and peroxisomes were purified by differential and density-gradient centrifugation using either Percoll or sucrose gradients. The yields obtained in intact chloroplasts and peroxisomes from Vigna were considerably higher than those achieved for Phaseolus. Purified chloroplasts only contained the Cu, Zn-SOD II isozyme, but in mitochondria both Mn-SOD and Cu, Zn-SOD I isozymes were present. In purified peroxisomes no SOD activity was detected. The absence of SOD activity in leaf peroxisomes from Vigna contrasts with results reported for the amide-metabolizing legume Pisum sativum L. where the occurrence of Mn-SOD was demonstrated in leaf peroxisomes (del Río et al. 1983. Planta 158: 216–224; Sandalio et al. 1987. Plant Sci. 51: 1–8). This suggests that in leaf peroxisomes from Vigna plants the generation of O2- radicals under normal conditions probably does not take place.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1991.tb00095.x
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