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Sayfa 1 itibaren 73 Sonuçlar
The impact of ozone on juvenile maize (Zea mays L.) plant photosynthesis: effects on vegetative biomass, pigmentation, and carboxylases (PEPc and Rubisco).
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The impact of ozone on crops was more studied in C (3) than in C (4) species. In C (3) plants, ozone is known to induce a photosynthesis impairment that can result in significant depressions in biomass and crop yields. To investigate the impact of O (3) on C (4) plant species, maize seedlings ( ZEA
Changes in PEP carboxylase, rubisco and rubisco activase mRNA levels from maize (Zea mays) exposed to a chronic ozone stress.
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We quantified the ozone impact on levels of Zea mays L. cv. Chambord mRNAs encoding C4-phosphoenolpyruvate carboxylase (C4-PEPc), ribulose-l,5-bisphosphate carboxylase/oxygenase small and large subunits (Rubisco-SSU and Rubisco-LSU, respectively) and Rubisco activase (RCA) using real-time RT-PCR.
Simultaneous determination of Rubisco carboxylase and oxygenase kinetic parameters in Triticum aestivum and Zea mays using membrane inlet mass spectrometry.
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The lack of complete Rubisco kinetic data for numerous species is partly because of the time consuming nature of the multiple methods needed to assay all of the Rubisco parameters. We have developed a membrane inlet mass spectrometer method that simultaneously determines the rate of Rubisco
Can the cold tolerance of C4 photosynthesis in Miscanthus x giganteus relative to Zea mays be explained by differences in activities and thermal properties of Rubisco?
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The previous investigations show that the amount and activity of Rubisco appears the major limitation to effective C(4) photosynthesis at low temperatures. The chilling-tolerant and bioenergy feedstock species Miscanthus x giganteus (M. x giganteus) is exceptionally productive among C(4) grasses in
Ozone tolerant maize hybrids maintain Rubisco content and activity during long-term exposure in the field
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Ozone pollution is a damaging air pollutant that reduces maize yields equivalently to nutrient deficiency, heat, and aridity stress. Therefore, understanding the physiological and biochemical responses of maize to ozone pollution and identifying traits predictive of ozone tolerance is important. In
The influence of light quality on C4 photosynthesis under steady-state conditions in Zea mays and Miscanthus×giganteus: changes in rates of photosynthesis but not the efficiency of the CO2 concentrating mechanism.
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Differences in light quality penetration within a leaf and absorption by the photosystems alter rates of CO(2) assimilation in C(3) plants. It is also expected that light quality will have a profound impact on C(4) photosynthesis due to disrupted coordination of the C(4) and C(3) cycles. To test
Rubisco Accumulation Factor 1 from Thermosynechococcus elongatus participates in the final stages of ribulose-1,5-bisphosphate carboxylase/oxygenase assembly in Escherichia coli cells and in vitro.
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Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) biosynthesis is a multi-step process in which specific chaperones are involved. Recently, a novel polypeptide, Rubisco Accumulation Factor 1 (RAF1), has been identified as a protein that is necessary for proper assembly of this enzyme in
Identification and metabolic characterization of the Zea mays mitochondrial homolog of the Escherichia coli groEL protein.
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We have characterized an abundant mitochondrial protein from Zea mays and have shown it to be structurally and metabolically indistinguishable from a previously described Tetrahymena thermophila and Saccharomyces cerevisiae mitochondrial protein, referred to as hsp60, which is homologous to the
Genetic Variability in Carbon Fixation, Sucrose-P-Synthase and ADP Glucose Pyrophosphorylase in Maize Plants of Differing Growth Rate.
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The net photosynthetic rate and the activities of ribulose 1,5 bisphosphate carboxylase (RubisCo), phosphoenolpyruvate carboxylase, sucrose-P-synthase, and ADP glucose-pyrophosphorylase, key enzymes of the leaf carbohydrate metabolism were compared in eight maize (Zea mays L.) genotypes presenting
Effect of trifluoroacetate, a persistent degradation product of fluorinated hydrocarbons, on Phaseolus vulgaris and Zea mays.
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The aim of this study was to quantify the effect of the pollutant, trifluoroacetate (TFA), on growth and photosynthesis of Phaseolus vulgaris (C(3)) and Zea mays (C(4)) in order to elucidate the physiological and biochemical basis of its inhibitory action. In whole plant studies, photosynthetic gas
Plant-derived sucrose is a key element in the symbiotic association between Trichoderma virens and maize plants.
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Fungal species belonging to the genus Trichoderma colonize the rhizosphere of many plants, resulting in beneficial effects such as increased resistance to pathogens and greater yield and productivity. However, the molecular mechanisms that govern the recognition and association between Trichoderma
[The immunogold localization of Rubisco and its activase in chloroplasts of barley and maize leaves].
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Cellular localization of Rubisco and Rubisco activase (RCA) in the C(3) plant barley (Hordeum vulgare L.) and the C(4) plant maize (Zea mays L.) leaves was investigated using immunogold-labeling electron microscopy. The results showed that the leaf anatomy and the immunolocalization of the two
Genetic engineering of maize (Zea mays) for high-level tolerance to treatment with the herbicide dicamba.
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Herbicide-tolerant crops have been widely and rapidly adopted by farmers in several countries due to enhanced weed control, lower labor and production costs, increased environmental benefits, and gains in profitability. Soon to be introduced transgenic soybean and cotton varieties tolerant to
RAF2 is a RuBisCO assembly factor in Arabidopsis thaliana.
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Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) catalyzes the reaction between gaseous carbon dioxide (CO2 ) and ribulose-1,5-bisphosphate. Although it is one of the most studied enzymes, the assembly mechanisms of the large hexadecameric RuBisCO is still emerging. In bacteria and in the
Species-dependent variation in the interaction of substrate-bound ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) and rubisco activase.
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Purified spinach (Spinacea oleracea L.) and barley (Hordeum vulgare L.) ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase supported 50 to 100% activation of substrate-bound Rubisco from spinach, barley, wheat (Triticum aestivum L.), soybean (Glycine max L.), pea (Pisum sativum L.),
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