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  • Chloroplast biogenesis  (2)
  • Antioxidant  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Planta 207 (1998), S. 313-324 
    ISSN: 1432-2048
    Schlagwort(e): Key words: Alpine plant ; Antioxidant ; Paraquat tolerance ; Photoinhibition ; Photorespiration ; Xanthophyll cycle
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract. Leaves of high-mountain plants were highly resistant to photoinhibitory damage at low temperature. The roles of different photoprotective mechanisms were compared. Mainly, the alpine species Ranunculus glacialis (L.) and Soldanella alpina were investigated because they appeared to apply greatly divergent strategies of adaptation. The ratio of electron transport rates of photosystem II/photosystem I measured in thylakoids from R. glacialis did not indicate a specific acclimation to high irradiance. Low rates of a chloroplast-mediated inactivation of catalase (EC 1.11.1.6) in red light indicated, however, that less reactive oxygen was released by isolated chloroplasts from R. glacialis than by chloroplasts from lowland plants. Leaves of S. alpina and of Homogyne alpina (L.) Cass, but not those of R. glacialis, had a very high capacity for antioxidative protection, relative to lowland plants, as indicated by a much higher tolerance against paraquat-mediated photooxidative damage and a higher -tocopherol content. Accordingly, ascorbate and glutathione were strongly oxidized and already largely destroyed at low paraquat concentrations in leaves of R. glacialis, but were much less affected in leaves of  S. alpina. Non-radiative dissipation of excitation energy was essential for photoprotection of leaves of  S. alpina and depended on the operation of the xanthophyll cycle. Strong non-photochemical quenching of chlorophyll fluorescence occurred also in R. glacialis leaves at high irradiance, but was largely independent of the presence of zeaxanthin or antheraxanthin. For R. glacialis, photorespiration appeared to provide a strong electron sink and a most essential means of photoprotection, even at low temperature. Application of phosphinothricin, which interferes with photorespiration by inhibition of glutamine synthetase, caused a striking reduction of electron transport through photosystem II and induced marked photoinhibition at both ambient and low temperature in leaves of R. glacialis, while  S. alpina was less affected.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    ISSN: 1432-2048
    Schlagwort(e): Chloroplast biogenesis ; Cytokinins ; Enzyme development ; Photoregulation ; Ribulose-1,5-bisphosphate carboxylase ; Secale
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The role of cytokinin in plastid biogenesis was investigated in etiolated rye leaves (Secale cereale L.) and compared with the effect of white light. Cytokinin deficiency of the leaves was induced by early excision of the seedling roots and reversed by the application of kinetin. The cytokinin supply had a much greater influence on plastid biogenesis than on leaf growth in general. The activities of several chloroplastic enzymes were increased 200%–400% after kinetin treatment of cytokinin-depleted leaves. The activity of ribulose-1,5-bisphosphate carboxylase (EC 4.1.1.39) and the amount of fraction-I protein even showed a sevenfold increase. In cytokinin-depleted leaves the development of ribulose-1,5-bisphosphate carboxylase and NADP-glyceraldehydephosphate dehydrogenase was specifically, and markedly inhibited by actinomycin D. The inhibition was partially or even completely overcome after treatment with kinetin. However, under all conditions, RNA synthesis of the leaves, was only partially inhibited by actinomycin D. According to immunologic studies, all dark-grown leaves, in addition to the complete enzyme, contained an excess of free small subunit of ribulose-1,5-bisphosphate carboxylase that was absent in mature light-grown leaves. The most striking accumulation of free small subunit, protein occurred in cytokinin-depleted dark-grown leaves, indicating a deficiency of the plastidic synthesis of the large subunit. The capacity as well as the activity of plastidic protein synthesis was preferentially increased by cytokinin and light. Cytokinin increased, the amount of plastidic ribosomes per leaf and relative to the amount of cytoplasmic ribosomes. While the percentage of cytoplasmic ribosomes bound as polyribosomes was little affected by the cytokinin supply, the proportion of plastidic polyribosomes was increased from 11% to 18% after kinetin treatment of cytokinin-depleted leaves. In the light, the proportion of plastidic polyribosomes reached 39% of the total plastidic ribosomes.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Planta 135 (1977), S. 83-88 
    ISSN: 1432-2048
    Schlagwort(e): Chlorophyll ; Chloroplast biogenesis ; High-temperature sensitivity ; Plastid ribosomes ; Ribosomes ; Secale
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The leaves of young rye plants (Secale cereale L.) grown at 32° were deficient in chlorophyll and in chloroplastic rRNA as compared to those grown at 22°, which developed normally. Both chlorophyll accumulation and the formation of plastidic rRNA were largely restored at 32° when the plants were transfered several times for 1 h per day to 22°. In the chlorotic 32°-grown rye leaves the in vivo activity of δ-aminolevulinate synthetase was very low. Aminolevulinate dehydratase however, exhibited high activity in extracts from 32°-grown leaves and was localized in the plastid fraction isolated from the chlorotic leaf tissue. After application of δ-aminolevulinic acid to chlorotic parts of leaves growing at 32°, protochlorophyll(ide) was formed and accumulated in the dark. In the light, the protochlorophyll(ide) was photooxidized at 32°. The results suggest a cytoplasmic site of synthesis for the series of enzymes converting δ-aminolevulinate to protochlorophyll(ide). It is concluded that an inhibition of δ-aminolevulinate synthetase and the photooxidation of protochlorophyll(ide) or chlorophyll are responsible for the chlorosis of the leaves at 32°.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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