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Diverted secondary metabolism and improved resistance to European corn borer (Ostrinia nubilalis) in maize (Zea mays L.) transformed with wheat oxalate oxidase.

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An alteration in the secondary metabolism of maize (Zea mays L.) genetically modified with the wheat oxalate oxidase (OxO) gene was observed using HPLC and fluorescence microscopy. Phenolic concentrations in the OxO lines were significantly increased, but DIMBOA synthesis was reduced due to a

Characterization of cell wall oxalate oxidase from maize roots.

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Oxalate oxidase activity was detected in the cell wall fraction isolated from maize roots (Zea mays L.). The enzyme was active at acidic pH with optimal activity at pH 3.2. It was thermally extremely stable and resistant to high salt concentration, SDS and pepsin. The enzyme activity was inhibited

Chelant-assisted phytoextraction and accumulation of Zn by Zea mays.

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Zea mays plants were exposed to soils with concentrations of Zn ranging from 64 to 1800 mg kg(-1) dw, and the efficiency of three selected chelating agents (trisodium citrate (CI), disodium oxalate (OX) and disodium dihydrogen ethylene-diamine-tetraacetate (EDTA)) in enhancing metal phytoextraction

A kinetic investigation of phosphoenolpyruvate carboxylase from Zea mays.

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The reaction catalyzed by phosphoenolpyruvate carboxylase from Zea mays has been studied kinetically. Results of initial velocity patterns and inhibition studies indicate that phosphoenolpyruvate carboxylase has a random sequential mechanism in which there is a high level of synergism in the binding

Maize Oxalyl-CoA Decarboxylase1 Degrades Oxalate and Affects the Seed Metabolome and Nutritional Quality.

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The organic acid oxalate occurs in microbes, animals, and plants; however, excessive oxalate accumulation in vivo is toxic to cell growth and decreases the nutritional quality of certain vegetables. However, the enzymes and functions required for oxalate degradation in plants remain largely unknown.

Flavin-containing polyamine oxidase is a hydrogen peroxide source in the oxidative response to the protein phosphatase inhibitor cantharidin in Zea mays L.

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In this study, the specific contribution of polyamine oxidase (PAO), a hydrogen peroxide (H2O2)-producing enzyme, to the oxidative burst induced in maize mesocotyl by the phosphatase inhibitor cantharidin was examined. For this purpose, a pharmacological approach was applied using, either in vitro

Novel Effects of Nanoparticulate Delivery of Zinc on Growth, Productivity, and Zinc Biofortification in Maize (Zea mays L.).

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In the present investigation, nanoscale zinc oxide particulates (ZnO-nanoparticulates) were prepared using a modified oxalate decomposition method. Prepared ZnO-nanoparticulates (mean size = 25 nm) were characterized using techniques such as transmission electron microscopy (TEM), Fourier transform

Chemical Analysis of Fermentable Sugars and Secondary Products in 23 Sweet Sorghum Cultivars.

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Sorghum (Sorghum bicolor (L.) Moench) is a heat- and drought-tolerant crop that has promise to supplement corn (Zea mays L.) for biofuel production from fermentable sugars (for sweet cultivars) and lignocellulosic biomass. Quantitative relationships are lacking to predict the accumulation of primary

Enzyme Profiles in Seedling Development and the Effect of Itaconate, an Isocitrate Lyase-directed Reagent.

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Changes in levels of isocitrate lyase, malate synthase, and catalase have been investigated during germination of flax (Linum usitatissimum L.) in the presence and absence of itaconate. Germination was accompanied by a rapid increase in these enzymes during the first 3 days. The presence of 38

Toxicity of naturally-contaminated manganese soil to selected crops.

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The impact of manganese excess using naturally contaminated soil (Mn-soil, pseudototal Mn 6494 vs 675 μg g(-1) DW in control soil) in the shoots of four crops was studied. Mn content decreased in the order Brassica napus > Hordeum vulgare > Zea mays > Triticum aestivum. Growth was strongly depressed

Altered metabolic hormones, impaired nitrogen retention, and hepatotoxicosis in lambs fed Kochia scoparia hay.

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Livestock grazing lush Kochia scoparia (L.) Schrad, sometimes experience BW loss, hyperbilirubinemia, photosensitization, and polyuria. Animals fed kochia hay may exhibit milder or negligible signs of toxicosis but fail to utilize nutrients efficiently. To characterize early aspects of kochia

The calcium uptake of the rat heart sarcoplasmic reticulum is altered by dietary lipid.

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Small amounts of dietary n-3 fatty acids can have dramatic physiological effects, including the reduction of plasma triglycerides and an elevation of cellular eicosapentanoic (EPA) and docosahexanoic acids (DHA) at the expense of arachidonic acid (AA). We investigated the effects of alterations in

Light activation of NADP malic enzyme in leaves of maize: marginal increase in activity, but marked change in regulatory properties of enzyme.

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This article reports the characteristics of light activation of NADP-malic enzyme (NADP-ME, EC 1.1.1.40) in leaf discs of maize (Zea mays cv. VMH 404) for the first time. The leaf discs were illuminated in the presence of 2 mmol/L bicarbonate, as light activation increases in the presence of

High aluminum resistance in buckwheat. Ii. Oxalic acid detoxifies aluminum internally

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Buckwheat (Fagopyrum esculentum Moench. cv Jianxi), which shows high Al resistance, accumulates Al in the leaves. The internal detoxification mechanism was studied by purifying and identifying Al complexes in the leaves and roots. About 90% of Al accumulated in the leaves was found in the cell sap,

Modelling of auxin-binding protein 1 suggests that its C-terminus and auxin could compete for a binding site that incorporates a metal ion and tryptophan residue 44.

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Sequence comparison indicates that auxin-binding protein 1 (ABP1) belongs to a family of proteins with the core beta-barrel structure of the vicilins. Previous modelling within this family correctly predicted metal-ion binding and oligomeric properties of oxalate oxidase. ABP1 also contains a

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Herbal & Natural Medicine

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