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  • 1
    Electronic Resource
    Electronic Resource
    Localization of glycolate dehydrogenase in two species of Dunaliella (1993)
    Springer
    Planta 191 (1993), S. 362-364 
    Details
    ISSN: 1432-2048
    Keywords: Dunaliella ; Glycolate dehydrogenase ; Glycolate oxidase ; Glycolate metabolism ; Peroxisome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The occurrence of glycolate oxidase in addition to glycolate dehydrogenase in Dunaliella salina and D. primolecta, as reported in the literature, could not be confirmed. Both species were demonstrated to possess only glycolate dehydrogenase. After separation of organelles by gradient centrifugation, glycolate dehydrogenase along with hydroxypyruvate reductase was found exclusively in the mitochondria. Thus the peroxisomes from Dunaliella are not of the leaf-type: because of their content of catalase, uricase and hydroxyacyl-CoA dehydrogenase they appear to be of the same type as in Eremosphaera and other chlorophycean algae. No activity of glycolate dehydrogenase was found in the chloroplast fraction when the 2,6-dichlorophenol-indophenol test was used.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00195694
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation and characterization of peroxisomes from diatoms (1995)
    Springer
    Planta 195 (1995), S. 403-407 
    Details
    ISSN: 1432-2048
    Keywords: Glycolate metabolism ; Nitzschia ; Perox ; isome ; Thalassiosira
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Peroxisomes were isolated by gradient centrifugation from two different diatoms: Nitzschia laevis (subgroup of Pennales) and Thalassiosira fluviatilis (subgroup of Centrales). In neither of these organelles could catalase or any H2O2-forming oxidase be demonstrated. The glycolate-oxidizing enzyme present in the peroxisomes is a dehydrogenase capable of oxidizing l-lactate as well. The peroxisomes also contain the glyoxysomal markers isocitrate lyase and malate synthase. However, enzymes of the fatty-acid β-oxidation pathway are located exclusively in the mitochondria. The mitochondria additionally possess glutamate-glyoxylate aminotransferase and a glycolate dehydrogenase which differs from the peroxisomal glycolate dehydrogenase since it preferably utilizes d-lactate as an alternative substrate. Hydroxypyruvate reductase and glyoxylate carboligase were not found in the cells of either diatom. By culturing Nitzschia laevis it could be demonstrated that decreasing the CO2 concentration in the aeration mixture from 2% to 0.03% and increasing the irradiance from 40 to 250 μmol quanta · m−2 · s−1 resulted in an increase of all peroxisomal enzyme activities. In addition, enzyme activities of the β-oxidation pathway were increased. However, mitochondrial glycolate dehydrogenase and aminotransferase did not alter their activities under these conditions. Summarizing all results, it is postulated that there are two different pathways for the metabolism of glycolate in the diatoms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00202598
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    Paper (German National Licenses)
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