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  • 1
    Electronic Resource
    Electronic Resource
    Literaturkarussell. Biologie (1996)
    Weinheim : Wiley-Blackwell
    Chemie in unserer Zeit 30 (1996), S. VI 
    Details
    ISSN: 0009-2851
    Keywords: Chemistry ; Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ciuz.19960300213
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  • 2
    Electronic Resource
    Electronic Resource
    Biologie (1995)
    Weinheim : Wiley-Blackwell
    Chemie in unserer Zeit 29 (1995), S. VI 
    Details
    ISSN: 0009-2851
    Keywords: Chemistry ; Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ciuz.19950290513
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  • 3
    Electronic Resource
    Electronic Resource
    Interdisziplinäres (1995)
    Weinheim : Wiley-Blackwell
    Chemie in unserer Zeit 29 (1995), S. XVIII 
    Details
    ISSN: 0009-2851
    Keywords: Chemistry ; Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ciuz.19950290518
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  • 4
    Electronic Resource
    Electronic Resource
    Wissenschaft (1995)
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 25 (1995), S. 346-347 
    Details
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/biuz.19950250605
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  • 5
    Electronic Resource
    Electronic Resource
    Correlations between photosynthetic enzymes, CO2-fixation and plastid structure in an albino mutant of Zea mays L. (1976)
    Springer
    Planta 131 (1976), S. 263-270 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary An albino seedling of Zea mays L. was investigated for its potential for CO2-assimilation. In the mesophyll the number, dimensions and fine structure of chloroplasts are drastically reduced but to a lesser extent in the bundle sheath. Chlorophyll concentration is zero and carotenoid concentration almost zero. Albinism also exerts a strong influence on the stroma of bundle sheath chloroplasts; ribulose-1.5-biphosphate carboxylase (EC 4.1.1.39) activity and glyceraldehyde-3-phosphate dehydrogenase (NADP) (EC 1.2.1.13) activity is not detectable. The C4-enzymes phosphoenolpyruvate carboxylase (EC 4.1.1.31) and malate dehydrogenase (decarboxylating) (EC 1.1.1.40) and the non-photosynthetic linked enzymes malate dehydrogenase (NAD) (EC 1.1.1.37), aspartate-2-oxoglutarate aminotransferase (EC 1.1.1.37), aspartate-2-oxoglutarate aminotransferase (EC 2.6.1.1.) and glyceraldehyde-3-phosphate dehydrogenase (NAD) (EC 1.2.1.1.) are present in the albino seedling with activities comparable to those in etiolated maize seedlings. The potential for CO2 fixation of the albino seedlings exceeds that of comparable dark seedlings considerably. The results are discussed with regard to enzyme localization of the C4 pathway of photosynthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00385424
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  • 6
    Electronic Resource
    Electronic Resource
    Photorespiration and β-carboxylation in brown macroalgae (1980)
    Springer
    Planta 150 (1980), S. 189-190 
    Details
    ISSN: 1432-2048
    Keywords: Brown algae ; β-Carboxylation ; Fucus ; Laminaria ; PEP-Carboxykinase ; Photorespiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Photorespiration has been assayed in a variety of marine macroalgae by the Warburg oxygen inhibitory effect and the percentage14C-labeling of glycine and serine. It was found that particularly the members of the brown macroalgae examined, such asFucus andLaminaria (Phaeophyceae), show a rather weak response to high O2 partial pressure. This observation is attributed to the appreciably high potential for β-carboxylation via PEP-carboxykinase, generally occurring in brown seaweeds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00582365
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  • 7
    Electronic Resource
    Electronic Resource
    CO2-Fixierung und Stofftransport in benthischen marinen Algen (1972)
    Springer
    Planta 103 (1972), S. 55-64 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary When discs punched out of the median part of the phylloid of Laminaria saccharina Lamour. were exposed to H14CO3 - in the light for periods of 10 sec to 10 min, 14C was rapidly incorporated into various photosynthetic products. As compared with dark fixation, 14C-photosynthesis increased exponentially during the first 60 sec of incubation in H14CO3 -. Fixation rates were found to be 76 μmol CO2·dm-2·h-1 or 100 μmol CO2·mg-1 chlorophyll a·h-1. Eighty-five per cent of the total 14C assimilated after 10 sec was fixed in phosphoglycerate and in the sugar monophosphates, 2% in the sugar diphosphates, and only 3.5% in malate and aspartate. While the radioactivity of malate and aspartate only rose to a constant level, the percentage of the total 14C in phosphoglycerate and-to a lower extent-that in the sugar monophosphates rapidly decreased with the duration of light exposure. Simultaneously, mannitol and glycine+serine became labelled with 43% and 32% respectively of the total 14C after 10 min light fixation. In the dark, the percentage of the total 14C in malate decreased with the time of H14CO2--incubation, while there was a remarkable increase in radioactivity of aspartate and glutamate. Within 60 min darkness no labelling of mannitol was found. From the present results it is concluded that the photosynthetic carbon cycle first described by Bassham and Calvin operates in Laminaria saccharina.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00394606
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  • 8
    Electronic Resource
    Electronic Resource
    Lokalisation der Mannitbiosynthese in der marinen Braunalge Fucus serratus (1973)
    Springer
    Planta 113 (1973), S. 173-178 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Tips of fronds of Fucus serratus L. were exposed to H14CO3 in the light for periods of 10, 30, 60, and 180s, fixed in petrol ether at-70° C, and subsequently lyophilized. Pheoplasts (=chloroplasts) were isolated using the nonaqueous technique of Thalacker et al. (1959). After extraction and chromatography percentage 14C activity and distribution of individual photoassimilates between pheoplasts and other compartments of assimilating cells were analyzed. Eighty percent of [14C]-phosphate esters were found within the pheoplasts after 10s 14C-assimilation, whereas only 25% were found there after 30s. After 10s [14C] mannitol is almost totally localized within the plastids, but after 180s the major part has been localized outside the pheoplasts. On the basis of these data the pheoplasts are regarded to be the only sites of primary mannitol biosynthesis during photosynthesis in Fucus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388201
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  • 9
    Electronic Resource
    Electronic Resource
    Carboxylating enzymes and pathway of photosynthetic carbon assmilation in different marine algae—Evidence for the C4-pathway? (1977)
    Springer
    Planta 133 (1977), S. 191-196 
    Details
    ISSN: 1432-2048
    Keywords: C4-pathway ; Dark fixation CO2 dark ; Marine macroalgae ; Photosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Experiments on short-term photosynthesis in H14CO3 - (2–5 s) using various species of different algal classes resulted in predominant 14C-labelling (〉90% of total 14C-incorporation) of phosphorylated compounds. The percentage of malate and aspartate usually accounts for distinctly less than 10% of the total 14C-labelling. These findings are consistent with data from enzymatic analyses, since 97–100% of the carboxylation capacity is due to ribulose-1.5-biphosphate carboxylase (EC 4.1.1.39) in Rhodophyceae and Chlorophyceae. Phaeophyceae are generally characterized by considerable activity of phosphoenolpyruvate carboxykinase (EC 4.1.1.32): at least 10% of carboxylation is confined to this enzyme. Similar ratios are obtained when rates of photosynthesis and of light-independent CO2-fixation are compared. Activity of phosphoenolpyruvate carboxylase (EC 4.1.1.31) could not be detected in the species investigated. The results are discussed with emphasis on the pathway of photosynthetic carbon assimilation in marine algae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00391918
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  • 10
    Electronic Resource
    Electronic Resource
    Carbon assimilation by different developmental stages of Laminaria saccharina (1979)
    Springer
    Planta 144 (1979), S. 497-501 
    Details
    ISSN: 1432-2048
    Keywords: Algae (brown) ; Carboxylation ; CO2 assimilation ; Laminaria ; Photosynthesis (laminaria)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Various stages of the life cycle of the marine brown alga Laminaria saccharina (L.) Lamour. (Laminariales, Phaeophyta) including male and female gametophytes, female gametes, zygotes and young sporophytes of different age were investigated for their potentials of carbon dioxide (14CO2) fixation. Rates of photosynthesis attain the same order of magnitude in all stages. Photosynthetic 14CO2-fixation is accompanied by a substantial light independent carbon assimilation. This is confirmed by rate determinations of the equivalent carboxylating enzymes present in the plants, ribulose-1,5-bisphosphate carboxylase (EC 4.1.1.39) and phosphoenolpyruvate carboxokinase (EC 4.1.1.32) as well as by chromatographic analyses of the appropriate [14C]-assimilate patterns.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00380129
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