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6 phosphogluconate dehydrogenase/paprastasis kukurūzas
Nuoroda įrašoma į mainų sritį
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Purification and characterization of cytosolic 6-phosphogluconate dehydrogenase isozymes from maize.
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Cytosolic isozymes of 6-phosphogluconate dehydrogenase were purified from roots of maize (Zea mays L.). The final preparation contained two 55-kD proteins. Affinity-purified dehydrogenases from a maize line that is null for both cytosolic 6-phosphogluconate dehydrogenase isozymes (Pgd1-null,
A survey for isoenzymes of glucosephosphate isomerase, phosphoglucomutase, glucose-6-phosphate dehydrogenase and 6-Phosphogluconate dehydrogenase in C3-, C 4-and crassulacean-acid-metabolism plants, and green algae.
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Two isoenzymes each of glucosephosphate isomerase (EC 5.3.1.9), phosphoglucomutase (EC 2.7.5.1), glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (EC 1.1.1.43) were separated by (NH4)2SO4 gradient solubilization and DEAE-cellulose ion-exchange chromatography from
Expression and distribution of cytosolic 6-phosphogluconate dehydrogenase isozymes in maize.
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Maize (Zea mays L.) cytosolic 6-phosphogluconate dehydrogenase isozymes (EC 1.1.1.44; 6-PGD) are encoded by unlinked loci Pgd1 and Pgd2. Two families from a Robertson's Mutator line were isolated which have no detectable expression of Pgd2. These Pgd2-null mutants and a Pgd1-null line were used to
Chloroplast-localized 6-phosphogluconate dehydrogenase is critical for maize endosperm starch accumulation.
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Plants have duplicate versions of the oxidative pentose phosphate pathway (oxPPP) enzymes with a subset localized to the chloroplast. The chloroplast oxPPP provides NADPH and pentose sugars for multiple metabolic pathways. This study identified two loss-of-function alleles of the Zea mays (maize)
Adaptor ligation-based polymerase chain reaction-mediated walking.
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An improved method of adaptor ligation PCR was developed for isolation of unknown sequences flanking a known DNA sequence. It was determined that the specificity of the adaptor ligation-based walking technique could be significantly enhanced by using uniquely blocked adaptors along with removal of
Lipogenic enzyme activities in primary cultures of adult mouse hepatocytes.
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The effects of various unsaturated fatty acids such as oleic (18:1n-9), linoleic (18:2n-6) and arachidonic (20:4n-6) on the activities of fatty acid synthetase (FAS), malic enzyme (ME), glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH) all were determined in
Enzyme activities associated with carcinogen metabolism in liver and nonhepatic tissues of rats maintained on high fat and food-restricted diets.
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The influence of high fat or food-restricted diets on key enzymes associated with polycyclic aromatic hydrocarbon metabolism was assessed in liver, lung, kidney and stomach of rats. Animals had access ad libitum to the AIN-76A purified diet (control) or were given 65% of the intake of controls for 3
Peroxisome proliferator perfluorodecanoic acid alters glutathione and related enzymes.
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Previously we have shown that treatment with the peroxisome proliferator perfluorodecanoic acid (PFDA) significantly increased hepatic reduced glutathione (GSH) content without altering the activity of selenium-glutathione peroxidase. In this study we examined some potential mechanisms by which PFDA
Effects of butylparaben on antioxidant enzyme activities and histopathological changes in rat tissues
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Butyl p-hydroxybenzoic acid, also known as butylparaben (BP), is one of the most common parabens absorbed by the skin and gastrointestinal tract and metabolised in the liver and kidney. Recent in vivo and in vitro studies have raised concern that BP causes reproductive, development, and teratogenic
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