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  • 1
    Electronic Resource
    Electronic Resource
    Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: purification and characterization (1991)
    s.l. : American Chemical Society
    Biochemistry 30 (1991), S. 4612-4619 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00232a036
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  • 2
    Electronic Resource
    Electronic Resource
    Evidence against H+−HCO 3 − symport as the mechanism for HCO 3 − transport in the cyanobacteriumAnabaena variabilis (1984)
    Springer
    The journal of membrane biology 79 (1984), S. 271-274 
    Details
    ISSN: 1432-1424
    Keywords: Anabaena ; bicarbonate transport ; cyanobacteria ; photosynthesis ; proton motive force
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The rate of inorganic carbon uptake and its steadystate accumulation ratio (intracellular/extracellular concentration) was determined in the cyanobacteriumAnabaena variabilis as a function of extracellular pH. The free energy of protons ( $$\Delta \overline \mu _{H^ - }$$ ) across the plasmalemma was calculated from determinations of membrane potential, and intracellular pH, as a function of the extracellular pH. While inward proton motive force decreased with increasing extracellular pH from 6.5 to 9.5, rate of HCO 3 − influx and its accumulation ration increased. The latter is several times larger than would be expected should HCO 3 − influx be driven by $$\Delta \overline \mu _{H^ + }$$ . It is concluded that HCO 3 − transport in cyanobacteria is not driven by the proton motive force.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871065
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  • 3
    Electronic Resource
    Electronic Resource
    Response of the cultivated tomato and its wild salt-tolerant relative Lycopersiconpennellii to salt-dependent oxidative stress: The root antioxidative system (2001)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 112 (2001), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The response of the antioxidant system to salt stress was studied in the roots of the cultivated tomato Lycopersicon esculentum Mill. cv. M82 (Lem) and its wild salt-tolerant relative L. pennellii (Corr.) D'Arcy accession Atico (Lpa). Roots of control and salt (100 mM NaCl)-stressed plants were sampled at various times after commencement of salinization. A gradual increase in the membrane lipid peroxidation in salt-stressed root of Lem was accompanied with decreased activities of the antioxidant enzymes: superoxide dismutase (SOD; EC 1.15.1.1), catalase (CAT; EC 1.11.1.6), ascorbate peroxidase (APX; EC 1.11.1.11) and decreased contents of the antioxidants ascorbate and glutathione and their redox states. In contrast, increased activities of the SOD, CAT, APX, monodehydroascorbate reductase (MDHAR; EC 1.6.5.4), and increased contents of the reduced forms of ascorbate and glutathione and their redox states were found in salt-stressed roots of Lpa, in which the level of membrane lipid peroxidation remained unchanged. It seems that the better protection of Lpa roots from salt-induced oxidative damage results, at least partially, from the increased activity of their antioxidative system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2001.1120405.x
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  • 4
    Electronic Resource
    Electronic Resource
    The peroxisomal glycolate oxidase gene is differentially expressed in yellow and white sectors of the DP1 variegated tobacco mutant (2000)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 110 (2000), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The DP1 variegated mutant of Nicotiana tabacum contains translationally defective plastids in its white (W) leaf sectors. In the present study a second type of pigment-deficient sector displaying a pale-yellow color (Y sectors) was discerned. Chlorophyll and carotenoids contents in both leaf sectors are very low, although the Y sectors contain twice the carotenoid content of the W sectors. Rubisco large subunit polypeptide content is low in the W sectors, while in the Y sectors its content is comparable to that in the green sectors. However, both leaf sector types do not show photosynthetic activity under ambient CO2 concentration. The W and Y sectors exhibit 40 and 50% reduction in the level of the mRNA encoding the peroxisomal glycolate oxidase (GLO) enzyme, respectively. However, in the W sectors GLO activity and protein levels reached only 30% of that in the green sectors while in the Y sectors they almost reached the green sectors levels. It is suggested that the reduction in GLO mRNA levels in the Y and W sectors is resulted from inhibition of the putative plastid to nucleus signal. Post-transcriptional mechanism(s) that also regulate GLO gene expression may explain the discrepancies between GLO mRNA and GLO protein levels, as observed between the W, Y and green leaf sectors of the DP1 mutant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2000.110116.x
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  • 5
    Electronic Resource
    Electronic Resource
    Inhibition of glucose transport by phenylglyoxal: Both dissipation of ΔpH and essential arginyl residues are involved (1998)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 102 (1998), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effects of the arginine modifying reagent phenylglyoxal (PGO) on solute transport was studied in two cellular systems: protoplasts isolated from the mesophyll of Vicia faba L. and XD cell suspension culture of Nicotiana tabacum L. cv. Xanthi. The solutes in the case of the protoplasts were the non-metabolizable glucose analog 3-O-methyl-D-glucose (MeG), and a non-metabolizable amino acid analog α-aminoisobutyric acid (AIB), whereas the solutes for the cell suspension were AIB and nitrate. Solute transport in both systems was rapidly inhibited by PGO. Exposure of the protoplasts to light enhanced the initial rate of MeG uptake. PGO rapidly inhibited MeG uptake in both the light and the dark, the half-time for inactivation being less than 3 min. Flux analysis of double-labeled MeG showed that initial MeG uptake was mediated mainly by the plasma membrane transport system and that it was inhibited by PGO. Maximal inhibition of initial MeG uptake rate was observed at PGO concentrations of 1 mM and above. PGO treatment altered rapidly the equilibrium distribution of the ΔpH probe dimethyloxazolidine (DMO) in both cellular systems, indicating dissipation of ΔpH between cell and medium. In the protoplasts, PGO inhibited both DMO and MeG uptake at pH 5.5; however, at pH 7.0, where ΔpH is minimal, only MeG uptake was inhibited. Our results suggest that PGO has two effects on glucose uptake: an indirect effect through ΔpH dissipation and a direct effect through interaction with essential arginyl residues in the glucose transporter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1998.1020213.x
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  • 6
    Electronic Resource
    Electronic Resource
    Salt stress induces up-regulation of an efficient chloroplast antioxidant system in the salt-tolerant wild tomato species Lycopersicon pennellii but not in the cultivated species (2002)
    Oxford, UK : Blackwell Science, Ltd
    Physiologia plantarum 115 (2002), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The response of the chloroplastic antioxidant system of the cultivated tomato Lycopersicon esculentum (Lem) and its wild salt-tolerant related species L. pennellii (Lpa) to NaCl stress was studied. An increase in H2O2 level and membrane lipid peroxidation was observed in chloroplasts of salt-stressed Lem. In contrast, a decrease in these indicators of oxidative stress characterized chloroplasts of salt-stressed Lpa plants. This differential response of Lem and Lpa to salinity, correlates with the activities of the antioxidative enzymes in their chloroplasts. Increased activities of total superoxide dismutase (SOD), ascorbate peroxidase (APX), monodehydroascorbate reductase (MDHAR), glutathione-S-transferase (GST), phospholipid hydroperoxide glutathione peroxidase (PHGPX) and several isoforms of non-specific peroxidases (POD) were found in chloroplasts of salt-treated Lpa plants. In these chloroplasts, in contrast, activity of lipoxygenase (LOX) decreased while in those of salt-stressed Lem it increased. Although total SOD activity slightly increased in chloroplasts of salt-treated Lem plants, differentiation between SOD types revealed that only stromal Cu/ZnSOD activity increased. In contrast, in chloroplasts of salt-treated Lpa plants FeSOD activity increased while Cu/ZnSOD activity remained unchanged. These data indicate that salt-dependent oxidative stress and damage, suffered by Lem chloroplasts, was effectively alleviated in Lpa chloroplasts by the selective up-regulation of a set of antioxidative enzymes. Further support for the above idea was supplied by leaf discs experiments in which pre-exposure of Lpa plants to salt-treatment conferred cross-tolerance to paraquat-induced oxidative stress while increased oxidative damage by paraquat-treatment was found in salt-stressed Lem plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2002.1150309.x
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  • 7
    Electronic Resource
    Electronic Resource
    Activities of SOD and the ascorbate-glutathione cycle enzymes in subcellular compartments in leaves and roots of the cultivated tomato and its wild salt-tolerant relative Lycopersicon pennellii (2000)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 110 (2000), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The activities of the ascorbate-glutathione cycle enzymes ascorbate peroxidase (APX), monodehydroascorbate reductase (MDHAR), dehydroascorbate reductase (DHAR) and glutathione reductase (GR) and SOD were studied in cell organelles of the cultivated tomato Lycopersicon esculentum (M82) and its wild salt-tolerant related species Lycopersicon pennellii (Lpa). All four enzymes of the ascorbate-glutathione cycle were present in chloroplasts/plastids, mitochondria and peroxisomes of leaf and root cells of both tomato species. In all leaf and root organelles of both species, the activity of MDHAR was similar to, or higher than, that of APX, while the activity of DHAR was one order of magnitude lower than that of MDHAR. Based on these results, it is suggested that in the organelles of both tomato species, ascorbate is regenerated mainly by MDHAR. In both tomato species, GR activity, and to a lesser extent DHAR activity, was found to reside in the soluble fraction of all leaf and root cell organelles, while APX and MDHAR activities were distributed between the membrane and soluble fractions. A higher SOD to APX activity ratio in all Lpa organelles was the major difference between the two tomato species. It is possible that this higher ratio contributes to the inherently better protection of Lpa from salt stress, as was previously reported.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2000.110106.x
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