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oxygenase/азиатски ориз

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СтатииКлинични изследванияПатенти
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Purification, crystallization and preliminary X-ray diffraction analysis of pathogen-inducible oxygenase (PIOX) from Oryza sativa.

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Pathogen-inducible oxygenase (PIOX) is a heme-containing membrane-associated protein found in monocotyledon and dicotyledon plants that utilizes molecular oxygen to convert polyunsaturated fatty acids into their corresponding 2R-hydroperoxides. PIOX is a member of a larger family of fatty-acid

OsMIOX, a myo-inositol oxygenase gene, improves drought tolerance through scavenging of reactive oxygen species in rice (Oryza sativa L.).

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Myo-inositol oxygenase (MIOX), a unique monooxygenase, catalyzes the oxidation of myo-inositol to d-glucuronic acid. However, the protective role of MIOX in plants against oxidative stress or drought stress remains unknown. In this study, the functional characterization of MIOX obtained from the

Molecular cloning and characterization of cDNAs encoding two isoforms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in rice (Oryza sativa L.).

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Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) activase catalyzes the activation of RuBisCO in vivo. Two full length cDNAs designated as OsrcaA1 and OsrcaA2 encoding two RuBisCO activase isoforms of 47 and 43 kDa, respectively, have been cloned and characterized. The two isoforms were 99%
Employing high-resolution two-dimensional electrophoresis (2-DE), we studied changes in the rice leaf protein patterns, in response to applied heavy and alkaline metals, important environmental pollutants in our surroundings. Drastic changes in 2-DE protein patterns after treatment with copper,

Heme-heme oxygenase 1 system is involved in ammonium tolerance by regulating antioxidant defence in Oryza sativa.

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Despite substantial evidence showing the ammonium-altered redox homeostasis in plants, the involvement and molecular mechanism of heme-heme oxygenase 1 (heme-HO1), a novel antioxidant system, in the regulation of ammonium tolerance remain elusive. To fill in these gaps, the biological function of

PE-1, Encoding Heme Oxygenase 1, Impacts Heading Date and Chloroplast Development in Rice ( Oryza sativa L.).

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The duration of the rice growth phase has always been an important target trait. The identification of mutations in rice that alter these processes and result in a shorter growth phase could have potential benefits for crop production. In this study, we isolated an early aging rice mutant, pe-1,

Effects of Copper Oxide Nanoparticles on the Growth of Rice (Oryza Sativa L.) Seedlings and the Relevant Physiological Responses.

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Rice (Oryza sativa L.), a major staple food for billions of people, was assessed for its phytotoxicity of copper oxide nanoparticle (CuO NPs, size < 50 nm). Under hydroponic condition, seven days of exposure to 62.5, 125, and 250 mg/L CuO NPs significantly suppressed the growth rate of

Domain structures of chlorophyllide a oxygenase of green plants and Prochlorothrix hollandica in relation to catalytic functions.

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Chlorophyll b is a photosynthetic antenna pigment found in prochlorophytes and chlorophytes. In chlorophytes, its biosynthesis regulates the photosynthetic antenna size. Chlorophyll b is synthesized from chlorophyll a in a two-step oxygenation reaction by chlorophyllide a oxygenase (CAO). In this

Carotenoid oxygenases involved in plant branching catalyse a highly specific conserved apocarotenoid cleavage reaction.

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Recent studies with the high-tillering mutants in rice (Oryza sativa), the max (more axillary growth) mutants in Arabidopsis thaliana and the rms (ramosus) mutants in pea (Pisum sativum) have indicated the presence of a novel plant hormone that inhibits branching in an auxin-dependent manner. The

Catalytic properties of rice alpha-oxygenase. A comparison with mammalian prostaglandin H synthases.

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Long-chain fatty acids can be metabolized to C(n)(-1) aldehydes by alpha-oxidation in plants. The reaction mechanism of the enzyme has not been elucidated. In this study, a complete nucleotide sequence of fatty acid alpha-oxygenase gene in rice plants (Oryza sativa) was isolated. The deduced amino

Enzymic Properties of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase Purified from Rice Leaves.

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The enzymic properties of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase purified from rice (Oryza sativa L.) leaves were studied. Rice RuBPcarboxylase, activated by preincubation with CO(2) and Mg(2+) like other higher plant carboxylases, had an activation equilibrium constant (K(c)K(Mg))

Three-dimensional analysis of the senescence program in rice (Oryza sativa L.) coleoptiles. Investigations of tissues and cells by fluorescence microscopy.

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The coleoptile of rice (Oryza sativa L. cv. Nippon-bare) emerges from an imbibed seed on day 2 after sowing. Then, it matures and senesces rapidly. For analysis of the senescence pattern within individual coleoptiles, we monitored the distribution of chlorophyll (Chl) in entire coleoptiles and in

Changes in growth CO2 result in rapid adjustments of ribulose-1, 5-bisphosphate Carboxylase/Oxygenase small subunit gene expression in expanding and mature leaves of rice

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The accumulation of soluble carbohydrates resulting from growth under elevated CO2 may potentially signal the repression of gene activity for the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (rbcS). To test this hypothesis we grew rice (Oryza sativa L.) under ambient (350 &mgr;L

Fe deficiency induced changes in rice (Oryza sativa L.) thylakoids.

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Iron deficiency is an important abiotic stress that limits productivity of crops all over the world. We selected a hybrid rice (Oryza sativa L.), LYPJ, which is super high-yield and widely cultured in China, to investigate changes in the components and structure of thylakoid membranes and

Rice gibberellin-binding phosphoprotein structurally related to ribulose-1,5-bisphosphate carboxylase/oxygenase activase.

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A gibberellin A (GA)-binding protein was identified from rice (Oryza sativa L.) leaves by a ligand-binding assay. The dissociation constant of GA-binding protein and GA complex was about 100 nM. This protein has a relative molecular mass of 47 000 and an isoelectric point of 5.1. The partial amino
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