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  • -bisphosphate carboxylase/oxygenase  (1)
  • Kormophyten  (1)
  • Pisum (senescence)  (1)
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  • 1
    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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  • 2
    Electronic Resource
    Electronic Resource
    Proteolytic cleavage of plant proteins by peroxisomal endoproteases from senescent pea leaves (1999)
    Springer
    Planta 209 (1999), S. 308-313 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Peroxisome ; Pisum (senescence) ; Proteolysis ; Ribulose-1 ; 5 ; -bisphosphate carboxylase/oxygenase ; Senescence ; Xanthine oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The degradation of peroxisomal and nonperoxisomal proteins by endoproteases of purified peroxisomes from senescent pea (Pisum sativum L.) leaves has been investigated. In our experimental conditions, most peroxisomal proteins were endoproteolytically degraded. This cleavage was prevented, to some extent, by incubation with 2 mM phenylmethylsulfonylfluoride, an inhibitor of serine proteinases. The peroxisomal enzymes glycolate oxidase (EC 1.1.3.1), catalase (EC 1.11.1.6) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) were susceptible to proteolytic degradation by peroxisomal endoproteases, whereas peroxisomal manganese superoxide dismutase (EC 1.15.1.1) was not. Ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) from spinach and urease (EC 3.5.1.5) from jack bean were strongly degraded in the presence of peroxisomal matrices. These results indicate that proteases from plant peroxisomes might play an important role in the turnover of peroxisomal proteins during senescence, as well as in the turnover of proteins located in other cell compartments during advanced stages of senescence. On the other hand, our data show that peroxisomal endoproteases could potentially carry out the partial proteolysis which results in the irreversible conversion of xanthine dehydrogenase into the superoxide-generating xanthine oxidase (EC 1.1.3.22). This suggests a possible involvement of the peroxisomal endoproteases in a regulated modification of proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050637
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