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glucose 6 phosphate dehydrogenase/pomme de terre
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Purification, characterization, and cDNA sequence of glucose-6-phosphate dehydrogenase from potato (Solanum tuberosum L.).
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Glucose-6-phosphate dehydrogenase (G6PDH, E.C. 1.1.1.49) has been purified from potato tuber at least 850-fold to apparent homogeneity as judged by SDS-PAGE. The enzyme was characterized by Km values of 260 microM for glucose-6-phosphate and 6 microM for NADP and a broad pH optimum between pH 7.5
Molecular characterization of the plastidic glucose-6-phosphate dehydrogenase from potato in comparison to its cytosolic counterpart.
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We report on the cloning of a plastidic glucose-6-phosphate dehydrogenase (EC 1.1.1.49) from higher plants. The complete sequence of the plastidic enzyme was obtained after rapid amplification of cDNA ends and comprises a putative plastidic transit peptide. Sequences amplified from leaf or root
Molecular characterization of a novel glucose-6-phosphate dehydrogenase from potato (Solanum tuberosum L.).
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We describe a novel G6PD cDNA from potato. The deduced amino acid sequence shares 77% identity with the known chloroplast enzyme, but only 47% with the corresponding cytosolic G6PDH. The sequence comprises the two cysteine residues conserved in other redox-regulated chloroplast G6PDH and a transit
Differential regulation of glucose-6-phosphate dehydrogenase isoenzyme activities in potato.
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In plants, Glc-6-phosphate dehydrogenase (G6PDH) isoenzymes are present in the cytosol and in plastids. The plastidic enzymes (P1 and P2) are subject to redox regulation, but mechanisms that adjust cytosolic G6PDH activity are largely unknown. We adopted a leaf disc system for monitoring the effects
Glucose-6-phosphate dehydrogenase from sweet potato: substrate-induced change in the sedimentation coefficient of the enzyme.
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Isolation and characterisation of a full-length genomic clone encoding a plastidic glucose 6-phosphate dehydrogenase from Nicotiana tabacum.
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We describe here the isolation and characterisation of the first full-length genomic clone encoding a plant glucose 6-phosphate dehydrogenase (G6PDH; EC 1.1.1.49) from Nicotiana tabacum L. cv Samsun. The gene was expressed in all tissues, including roots, leaves, stems and flowers. Comparison of the
Correlation of viral RNA biosynthesis with glucose-6-phosphate dehydrogenase activity and host resistance.
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Changes in glucose-6-phosphate dehydrogenase (G6P DH; EC 1.1.1.49) activity caused by infection of tobacco ( Nicotiana tabacum L.) leaves with potato virus Y (PVY), cucumber mosaic virus, potato virus X, tobacco rattle virus and turnip mosaic virus, the subcellular localisation of G6P DH isozymes in
Glutamate synthesis in barley roots: the role of the plastidic glucose-6-phosphate dehydrogenase.
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Evidence is provided for a close link between glutamate (Glu) synthesis and the production of reducing power by the oxidative pentose phosphate pathway (OPPP) in barley ( Hordeum vulgare L. var. Alfeo) root plastids. A rapid procedure for isolating organelles gave yields of plastids of over 30%, 60%
Can Indirect Herbicide Exposure Modify the Response of the Colorado Potato Beetle to an Organophosphate Insecticide?
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Organisms live in complex multivariate environments. In agroecosystems, this complexity is often human-induced as pest individuals can be exposed to many xenobiotics simultaneously. Predicting the effects of multiple stressors can be problematic, as two or more stressors can have interactive
Specific expression of glucose-6-phosphate dehydrogenase (G6PDH) gene by salt stress in wheat (Triticum aestivum L.).
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We isolated three kinds of full-length cDNA clones for glucose-6-phosphate dehydrogenase (G6PDH) from wheat. They showed over 80% sequence homology with potato and alfalfa at the amino acid level, suggesting that the genes are highly conserved in angiosperms. The lack of a plastidic signal sequence,
Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase.
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The cDNA sequences encoding cytosolic and light-modulated plastidic glucose-6-phosphate dehydrogenase (G6PDH) from potato were modified by polymerase chain reaction and subsequently overexpressed in Escherichia coli. Characterization of the recombinant enzymes showed that they closely resembled
In situ staining of activities of enzymes involved in carbohydrate metabolism in plant tissues.
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A powerful technique is described to localize the activities of a range of enzymes in a wide variety of plant tissues. The method is based on the coupling of the enzymatic reaction to the reduction of NAD and subsequent reduction and precipitation of nitroblue tetrazolium. Enzymes that did not
The effect of phytic acid on the levels of blood glucose and some enzymes of carbohydrate and lipid metabolism.
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In this study, six groups of rats were fed as follows: Groups 1 and 2 were fed formulated diets supplemented with zinc or without zinc respectively. Groups 3 and 4 were fed formulated diets supplemented with zinc plus phytic acid extracted from sweet potato (Ipomea batatas) or commercial phytic acid
Transition of metabolisms in living popular bark from growing to wintering stages and vice versa: changes in glucose 6-phosphate and 6-phosphogluconate dehydrogenase activities and in the levels of sugar phosphates.
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Activities of glucose 6-phosphate, 6-phosphogluconate, and isocitrate dehydrogenases, together with intermediate levels of the glycolytic pathway and the pentose phosphate cycle, were measured throughout a year in the living bark of poplar (Populus gelrica). Shoots, immediately after budding (early
Protective effects of glucose-6-phosphate and NADP against alpha-chaconine-induced developmental toxicity in Xenopus embryos.
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In previous studies a metabolic activation system (MAS) composed of Aroclor 1254-induced rat liver microsomes led to an apparent reduction of potato glycoalkaloid developmental toxicity in the frog embryo teratogenesis assay-Xenopus (FETAX). The reasons for this reduction were investigated in this
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