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Seite 1 von 177 Ergebnisse
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
Isolation of Bundle Sheath Cell Chloroplasts from the NADP-ME Type C(4) Plant Zea mays: Capacities for CO(2) Assimilation and Malate Decarboxylation.
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Bundle sheath chloroplasts have been isolated from Zea mays leaves by a procedure involving enzymic digestion of mechanically prepared strands of bundle sheath cells followed by gentle breakage and filtration. The resulting crude chloroplast preparation was enriched by Percoll density layer
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
CO(2) Assimilation and Malate Decarboxylation by Isolated Bundle Sheath Chloroplasts from Zea mays.
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Conditions for optimal CO(2) fixation and malate decarboxylation by isolated bundle sheath chloroplasts from Zea mays were examined. The relative rates of these processes varied according to the photosynthetic carbon reduction cycle intermediate provided. Highest rates of malate decarboxylation,
Ligand binding on to maize (Zea mays) malate synthase: a structural study.
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A kinetic and ligand binding study on maize (Zea mays) malate synthase is presented. It is concluded from kinetic measurements that the enzyme proceeds through a ternary-complex mechanism. Michaelis constants (Km,glyoxylate and Km,acetyl-CoA) were determined to be 104 microM and 20 microM
The Involvement of Aspartate and Glutamate in the Decarboxylation of Malate by Isolated Bundle Sheath Chloroplasts from Zea mays.
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Aspartate or glutamate stimulated the rate of light-dependent malate decarboxylation by isolated Zea mays bundle sheath chloroplasts. Stimulation involved a decrease in the apparent K(m) (malate) and an increased maximum velocity of decarboxylation. In the presence of glutamate other dicarboxylates
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
Purification of the glyoxylate cycle enzyme malate synthase from maize (Zea mays L.) and characterization of a proteolytic fragment.
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A purification scheme is described for the glyoxylate cycle enzyme malate synthase from maize scutella. With our procedure, large amounts of extremely pure enzyme can easily be prepared. Purification involves a heat denaturation step, followed by ammonium sulfate precipitation, and chromatography on
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.
Relationships between Carbon Dioxide, Malate, and Nitrate Accumulation and Reduction in Corn (Zea mays L.) Seedlings.
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The observation that exposure of the leaf canopy to increasing concentrations of CO(2) (100-400 mul/l) decreases the influx of nitrate to the leaf blades, but not to the roots or stalks (largely leaf sheaths), was reconfirmed using (15)NO(3) (-). Decreases in leaf nitrate supply were associated with
Purification and crystallization of three isoenzymes of malate dehydrogenase from Zea mays seed.
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Aspartate stimulation of malate decarboxylation in Zea mays bundle sheath cells: possible role in regulation of C4 photosynthesis.
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Malate dehydrogenase in Zea mays: properties and inhibition by sulfite.
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