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  • 1970-1974  (7)
  • 1950-1954  (4)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 210 (1973), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary After illumination intact leaves of Zea mays contain sucrose and starch. The latter is located mainly in the bundle sheath cells. When 0.5 mm wide leaf strips are incubated with sucrose solution, the starch deposit in the bundle-sheath chloroplasts is greatly increased by light. When isolated bundle sheath cells are suspended in water or solutions of sucrose and various metabolites they are not capable of synthesizing starch. An appreciable production of starch in the chloroplasts of isolated bundle sheath cells can be observed only in the presence of glucose-1-phosphate.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Planta 96 (1971), S. 224-237 
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary O2-uptake and CO2-release by a chlorophyll-free, carotenoid-containing mutant of Chlorella vulgaris increase on addition of Na-glycolate by factors of 4–5 and 5–6, respectively (Fig. 1). In an enzyme preparation of that alga (sonification, centrifugation, precipitation with 0–30% (NH4)2SO4, dialysis) activity of glycolate oxidase can be demonstrated by O2-uptake (Fig. 2a) as well as by reduction of the artificial electron acceptor DCPIP (Fig. 2b). The same holds true for whole cells as well as equally prepared enzyme preparations of heterotrophically or autotrophically grown wildtype Chlorella vulgaris, provided the cells are cracked by a “French press” instead of a sonicator (Figs. 3a-c and 4a-c). Glyoxylate is the main reaction product (Table). Oxidation of exogenous glycolate is rapidly performed by whole cells of Scenedesmus quadricauda and of Ankistrodesmus convolutus, too, but hardly or not at all by Chlorella pyrenoidosa and Ankistrodesmus braunii. No definite influence of the level of CO2 applied during growth is found: Chlorella vulgaris and Ankistrodesmus convolutus show a rapid oxidation of glycolate after growth under 0,03 and 1,5% CO2 in air, whereas Chlorella pyrenoidosa and Ankistrodesmus braunii do not show an enhanced O2-uptake on addition of glycolate after either condition (Fig. 5). Various developmental stages of Chlorella pyrenoidosa respond differently to addition of glycolate, the extra O2-consumption varying between about 25% (mature cells) and 50–60% (young cells) of the endogenous rate (Fig. 6). It thus appears that species of unicellular green algae within the same genus have strong or weak glycolate oxidase activity and that several external factors have only a modifying effect on that enzyme.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Planta 99 (1971), S. 230-239 
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The effect of compounds on the activity of ammonium sulphate preparations of glycollate oxidase from Nicotiana tabacum cv. John Williams' Broadleaf and the aurea mutant Su/su is reported. Coupling to DCPIP as terminal oxidant under anaerobic conditions gave greater rates of glycollate oxidation than when measured as O2 uptake in the presence of cyanide. The enzyme also linked to DCPIP in the presence of O2, showing that it is a facultative aerobic dehydrogenase. Catalytic amounts of PMS stimulated enzyme-dependent oxygen uptake and DCPIP reduction under aerobic and anaerobic conditions. This further suggests that an intermediate carrier, or alternate acceptor, depending on concentration, exists before O2 in vivo. Naturally occurring quinoid compounds may fulfill such a role, as evidenced by the enhancement of aerobic DCPIP reduction upon addition of catalytic amounts of caffeic and chlorogenic acid. The observation that PMS, caffeic and chlorogenic acid, biopterin, 6-hydroxy-2-amino-4-hydroxypteridine and a quinone extract of N. tabacum quenched the inhibitory effect of blue light on tobacco glycollate oxidase, is in accordance with the possible function of such compounds in glycollate oxidation.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 81 (1972), S. 264-272 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Isopycnic sucrose density gradient centrifugation of cell-free extracts of a yellow mutant of Chlorella vulgaris and its green parent strain showed a distribution of catalase and glycollate oxidoreductase activity consistent with their association with a particle/organelle fraction. Gradient centrifugation starting from a pellet of cell-free material resulted in a concentration of enzyme activity in the 1.5 M to 2.0 M sucrose fractions which coincided with a microbody-containing fraction as determined by electron microscopy. The algal glycollate-oxidizing enzyme coupled to oxygen, oxidized both d- and l-lactate and was insensitive to cyanide in vitro, showing it to be similar to that of higher plants. The association of glycollate oxidase together with catalase, with the microbody fraction, may be taken as evidence for the presence of algal peroxisomes in these organisms.
    Type of Medium: Electronic Resource
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  • 6
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    Unknown
    Köln : Periodicals Archive Online (PAO)
    Zeitschrift für Religions- und Geistesgeschichte. 6 (1954) 138 
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  • 7
    facet.materialart.
    Unknown
    Köln : Periodicals Archive Online (PAO)
    Zeitschrift für Religions- und Geistesgeschichte. 6 (1954) 79 
    ISSN: 0044-3441
    Topics: History , Philosophy , Theology and Religious Studies
    Notes: Miscellanea
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  • 8
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. The presence of microbodies in the yellow mutant Chlorella vulgaris 211-2-11 h/20 has been demonstrated by means of electron microscopy. 2. A microbody preparation, obtained from the algae by cell disruption and subsequent sucrose density gradient centrifugation, contained an enzyme pattern which suggests that the microbodies from glucose-grown cells are of the peroxisomal rather than of the glyoxysomal type. No malate synthetase and no isocitrate lyase were found. 3. Microbodies of acetate-grown cells also did not contain isocitrate lyase or malate synthetase activities. In contrast to glucose-grown cells a supernatant fraction of acetate-grown cells exhibited low isocitrate lyase activity, but just as in the case of glucose-grown cells activity of malate synthetase was not detectable even if assayed for with a variety of methods, including the use of 14C-1-acetate. 4. In acetate-grown cells malate was the major product of acetate assimilation as evidenced by the characterization of short-term products of 14C-acetate assimilation. Malate was not a primary product of 14C-acetate assimilation in glucose-grown cells. 5. Since on the one hand the presence of malate synthetase could not be demonstrated in acetate-grown cells as well as in glucose-grown cells, on the other hand malate was the primary product of 14C-acetate assimilation in acetate-grown cells it must be concluded, either that the enzyme is so sensitive that it does not survive isolation, or that the mutant utilizes a pathway other than the glyoxylate by-pass for acetate assimilation when dependent upon acetate for growth. 6. As previously demonstrated (Codd et. al., 1972) the isolated microbodies from glucose-grown cells contain high amounts of catalase. An attempt to localize catalase cytochemically by the diaminobenzidine technique failed: diaminobenzidine plus H2O2 stained the microbodies, the mitochondria, Golgi apparatus, and even the lamellar system of the chlorophyll-free plastid. Staining of both the microbodies and mitochondria was relieved by aminotriazole.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Planta 116 (1974), S. 347-359 
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In tomato, pea, and maize roots, the presence of sucrose synthetase (E.C. 2.4.1.13), sucrose phosphate synthetase (E.C. 2.4.1.14), and both the alkaline and acid sucrases (E.C. 3.2.1.? and E.C. 3.2.1.26) could be demonstrated. The activity of these enzymes was measured directly on root slices suspended in the incubation mixture, which also contained 10% dimethyl sulfoxide or 5% ethyl acetate. These two additives increase the permeability of the membranes, thus allowing the entry of substrates to the site where the enzymes are located and favouring the release of products into the medium. The values found by measuring the activities of sucrose synthetase and the alkaline sucrase on tomato root were quite comparable to those obtained using enzymic preparations of the same tissue. In the case of the weakly active sucrose phosphate synthetase and the very active acid sucrase, the comparison of the two methods showed that losses of activity occurred during the preparation of the enzymes. By separating stele from cortex in tomato and maize roots, it could be shown that sucrose phosphate synthetase is located only in the stele, while the other enzymes are unevenly distributed between the two tissues, the sucrases predominating in the cortex. Sucrose phosphate synthetase and sucrose synthetase are most active in the region with root hairs of maize roots, while the activity of both sucrases is higher in the region near the apex. The highest invertase activity was measured in the apex of stem-borne adventitious roots that had not yet penetrated the soil. In older roots, sucrose phosphate synthetase disappears and the activity of all the other enzymes diminishes. It is suggested that the high activity of sucrose synthetase is present in the regions where an active synthesis of cell wall substances from glycosyl nucleotides is taking place, while the sucrases provide the initial substrates for most of the other pathways.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Journal of ornithology 93 (1952), S. 174-175 
    ISSN: 1439-0361
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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