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malate dehydrogenase/maíz
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Regulation of C4 photosynthesis: physical and kinetic properties of active (dithiol) and inactive (disulfide) NADP-malate dehydrogenase from Zea mays.
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NADP-malate dehydrogenase was purified from leaves of Zea mays in the absence of thiol-reducing agents by (NH4)2SO4, polyethylene glycol, and pH fractionation followed by dye-ligand affinity chromatography and gel filtration. The purified enzyme is completely inactive (no activity detected between
Amino Acid Sequence and Molecular Weight of Native NADP Malate Dehydrogenase from the C(4) Plant Zea mays.
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N-terminus amino acid analysis of purified corn (Zea mays) NADP malate dehydrogenase showed that the mature protein begins at serine-41 of the preprotein sequence and not threonine-58 as previously concluded; therefore, the transit peptide consists of 40 amino acids. The theoretical molecular weight
Plasma membrane-associated malate dehydrogenase of maize (Zea mays L.) roots: native versus recombinant protein.
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Malate dehydrogenase (MDH, EC 1.1.1.37) is involved in several cellular processes including plant development, nutrient uptake and oxidative stress. Evidence for a plasma membrane-associated MDH has been presented for maize (Zea mays L.) roots. In the present study isoenzymes of MDH were purified
NADP-malate dehydrogenase from leaves of Zea mays: purification and physical, chemical, and kinetic properties.
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NADP-malate dehydrogenase (NADP-MDH) from leaves of Zea mays has been purified and has a specific activity of 600-1000 mumol/min/mg protein. The native, inactive form of the enzyme is an 87.4-kDa, dimeric protein with a sedimentation coefficient of 5.5 S and a Stokes' radius of 3.62 nm. Isofocus
Duplicated cytosolic malate dehydrogenase genes in Zea mays.
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Six inbred lines of Zea mays expressing different soluble (cytosolic) malate dehydrogenase (sMDH) zymogram phenotypes were analyzed genetically. sMDH was found to be coded for by unlinked duplicated loci in four of these inbred lines. The remaining two lines were found not to possess these
Chromosomal Location of Two Mitochondrial Malate Dehydrogenase Structural Genes in ZEA MAYS Using Trisomics and B-A Translocations.
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Maize mitochondrial malate dehydrogenase is coded by four genetic loci, Mdh1, Mdh2, Mdh3 and Mdh4. Two of the four loci have been located on the long arm of chromosome 6, using trisomic analysis and B-A translocations.
Purification and crystallization of three isoenzymes of malate dehydrogenase from Zea mays seed.
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Malate dehydrogenase in Zea mays: properties and inhibition by sulfite.
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Mitochondrial malate dehydrogenase from corn : purification of multiple forms.
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A method to fractionate corn (Zea mays L. B73) mitochondria into soluble proteins, high molecular weight soluble proteins, and membrane proteins was developed. These fractions were analyzed by both sodium dodecyl sulfate-polyacrylamide gel electrophoresis and assays of mitochondrial enzyme
A gene modifying mitochondrial malate dehydrogenase isozymes in Sorghum (Gramineae).
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Malate dehydrogenase (MDH) isozymes extracted from dark-grown seedlings of Sorghum species are encoded by at least two genes with their products localized in the mitochondria (mt) and one gene with its products localized in the cytosol. In homozygous genotypes, the three mt-MDH isozymes represent
Hydrolysis of phosphoenolpyruvate catalyzed by phosphoenolpyruvate carboxylase from Zea mays.
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In addition to the normal carboxylation reaction, phosphoenolpyruvate carboxylase from Zea mays catalyzes a HCO3(-)-dependent hydrolysis of phosphoenolpyruvate to pyruvate and Pi. Two independent methods were used to establish this reaction. First, the formation of pyruvate was coupled to lactate
Activation of NADP-Malate Dehydrogenase, Pyruvate,Pi Dikinase, and Fructose 1,6-Bisphosphatase in Relation to Photosynthetic Rate in Maize.
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The activity and extent of light activation of three photosynthetic enzymes, pyruvate,Pi dikinase, NADP-malate dehydrogenase (NADP-MDH), and fructose 1,6-bisphosphatase (FBPase), were examined in maize (Zea mays var Royal Crest) leaves relative to the rate of photosynthesis during induction and
Phosphoproteome and proteome analyses reveal low-phosphate mediated plasticity of root developmental and metabolic regulation in maize (Zea mays L.).
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Phosphate (Pi) deficiency has become a significant challenge to worldwide agriculture due to the depletion of accessible rock phosphate that is the major source of cheap Pi fertilizers. Previous research has identified a number of diverse adaptive responses to Pi starvation in the roots of higher
Regulation of NADP-malate dehydrogenase in C4 plants: effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems.
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Activation and inactivation of NADP-malate dehydrogenase purified from Zea mays leaves were followed in a reconstituted system provided with thioredoxin poised in various redox states with dithiothreitol. The initial rate of activation or inactivation of NADP-malate dehydrogenase was proportional to
Regulation of NADP-malate dehydrogenase in C4 plants: relationship among enzyme activity, NADPH to NADP ratios, and thioredoxin redox states in intact maize mesophyll chloroplasts.
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NADP-malate dehydrogenase activity, the ratio of NADPH to NADP, and thioredoxin redox state in Zea mays chloroplasts were determined after various treatments. Following transfer from dark to light, NADP-malate dehydrogenase was activated more than 20-fold within 10 min while the proportion of
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