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superoxide dismutase/тутун
Врската е зачувана во таблата со исечоци
Страница 1 од 119 резултати
Isolation and characterization of cytosolic copper/zinc superoxide dismutase from Capsicum annuum L.
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A cDNA clone for a cytosolic Cu/Zn superoxide dismutase (Cu/ZnSOD) was isolated and characterized from red pepper (Capsicum annuum L.). The clone consisted of 735 bp containing one open reading frame (ORF) of 459 bp, 46 bp of 5'- and 230 bp of 3'-untranslated region. The nucleotide sequence of the
Isolation and characterization of mitochondrial manganese superoxide dismutase (MnSOD) from Capsicum annuum L.
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A cDNA clone for a mitochondrial manganese superoxide dismutase (MnSOD) was isolated and characterized from red pepper (Capsicum annuum L.). The clone consisted of 941 bp containing one open reading frame (ORF) of 687 bp, 34 bp/220 bp of 5'/3'-untranslated region. Amino acid sequence of the ORF
Differential expression of CuZn- and Fe-superoxide dismutase genes of tobacco during development, oxidative stress, and hormonal treatments.
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Chloroplasts of Nicotiana tabacum have two superoxide dismutases: a Fe- and a CuZn-containing enzyme, encoded by the nuclear genes sodB and sodCp, respectively. As a first step in studying the physiological function of these two enzymes, we compared the expression of sodB and sodCp in different
Paraquat tolerance of transgenic Nicotiana tabacum with enhanced activities of glutathione reductase and superoxide dismutase.
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Transgenic tobacco with enhanced cytosolic activities of glutathione reductase and superoxide dismutase were generated by cross-fertilization. Leaves of the hybrids exhibited further increased tolerance to a O2-.-generating herbicide paraquat than those of their parents. This result indicates the
Superoxide dismutase and peroxidase are coordinately regulated in differentiated and transformed tissues of Nicotiana tabacum.
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We used a series of normal and Agrobacterium-transformed, bacteria-free tobacco tissue cultures which differ in their levels of histodifferentiation to test the relationship of superoxide dismutase, peroxidase, and catalase to oncogenic transformation and differentiation. When compared with normal
Characterization of photosystem II in transgenic tobacco plants with decreased iron superoxide dismutase.
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Iron superoxide dismutases (FeSODs) play an important role in preventing the oxidative damage associated with photosynthesis. To investigate the mechanisms of FeSOD in protection against photooxidative stress, we obtained transgenic tobacco (Nicotiana tabacum) plants with severely decreased FeSOD by
Tissue-specific activity of two manganese superoxide dismutase promoters in transgenic tobacco.
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In eukaryotes, manganese superoxide dismutase is a nuclear-encoded protein that scavenges superoxide radicals in the mitochondrial matrix. We have isolated two manganese superoxide dismutase genes from Nicotiana plumbaginifolia L. and fused the 5' upstream regulatory region of these genes to the
Overproduction of petunia chloroplastic copper/zinc superoxide dismutase does not confer ozone tolerance in transgenic tobacco.
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Transgenic tobacco (Nicotiana tabacum cultivar W38) plants that overproduce petunia chloroplastic Cu/Zn superoxide dismutase were exposed to ozone dosages that injure control tobacco plants. Based on foliar injury ratings, there was no consistent protection provided to the transgenic plants. These
Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts.
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A chimeric gene consisting of the coding sequence for chloroplastic Fe superoxide dismutase (FeSOD) from Arabidopsis thaliana, coupled to the chloroplast targeting sequence from the pea ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit, was expressed in Nicotiana tabacum cv Petit Havana
Superoxide dismutase enhances tolerance of freezing stress in transgenic alfalfa (Medicago sativa L.).
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Activated oxygen or oxygen free radicals have been implicated in a number of physiological disorders in plants including freezing injury. Superoxide dismutase (SOD) catalyzes the dismutation of superoxide into O2 and H2O2 and thereby reduces the titer of activated oxygen molecules in the cell. To
Properties of purified cytosolic isoenzyme I of Cu,Zn-superoxide dismutase from Nicotiana plumbaginifolia leaves.
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The isoenzyme I of cytosolic Cu,Zn-superoxide dismutase (SOD) from Nicotiana plumbaginifolia (tobacco) leaves has been purified to apparent homogeneity. The relative molecular mass of the native isoenzyme, determined by gel filtration chromatography, is about 33.2 kDa. SDS-polyacrylamide gel
The induction of manganese superoxide dismutase in response to stress in Nicotiana plumbaginifolia.
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Superoxide dismutases (SODs) are metalloproteins that catalyse the dismutation of superoxide radicals to oxygen and hydrogen peroxide. The enzyme has been found in all aerobic organisms examined, where it plays a major role in the defence against toxic reduced oxygen species which are generated in
Developmental and environmental regulation of the Nicotiana plumbaginifolia cytosolic Cu/Zn-superoxide dismutase promoter in transgenic tobacco.
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Superoxide dismutases (SODs) play a key role in the cellular defense against reactive oxygen species. To study the transcriptional regulation at the cellular level, the promoter of the Nicotiana plumbaginifolia cytosolic gene encoding Cu/ZnSOD (SODCc) was fused to the beta-glucuronidase (GUS)
Redox-activated expression of the cytosolic copper/zinc superoxide dismutase gene in Nicotiana.
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Superoxide dismutases (SODs; superoxide: superoxide oxidoreductase, EC 1.15.1.1) play a key role in protection against oxygen radicals, and SOD gene expression is highly induced during environmental stress. To determine the conditions of SOD induction, the promoter of the cytosolic copper/zinc SOD
A plant manganese superoxide dismutase is efficiently imported and correctly processed by yeast mitochondria.
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In the plant Nicotiana plumbaginifolia, manganese superoxide dismutase (MnSOD) is synthesized in the cytoplasm as a preprotein and is subsequently translocated to the mitochondrial matrix with corresponding cleavage of an NH2-terminal leader sequence. To determine whether the plant enzyme could
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