hordeum californicum/phosphatase

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Characteristics of a photorespiratory mutant of barley (Hordeum vulgare L.) deficient in phosphogly collate phosphatase.

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A barley mutant RPr84/90 has been isolated by selecting for plants which grow poorly in natural air, but normally in air enriched to 0.8% CO2. After 5 minutes of photosynthesis in air containing(14)CO2 this mutant incorporated 26% of the(14)C carbon into phosphoglycollate, a compound not normally

Wheat (Triticum aestivum L.) and barley (Hordeum vulgare L.) multiple inositol polyphosphate phosphatases (MINPPs) are phytases expressed during grain filling and germination.

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At present, little is known about the phytases of plant seeds in spite of the fact that this group of enzymes is the primary determinant for the utilization of the major phosphate storage compound in seeds, phytic acid. We report the cloning and characterization of complementary DNAs (cDNAs)

Separation of the Mg-ATPases from the Ca-Phosphatase Activity of Microsomal Membranes Prepared from Barley Roots.

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Two methods for preparing membrane fractions from barley (Hordeum vulgare cv California Mariout 72) roots were compared in order to resolve reported differences between the characteristics of the plasma membrane ATPase of barley and that of other species. When microsomal membranes were prepared by a

Cytochemical localization of phosphatase in barley aleurone cells: The pathway of gibberellic-acid-induced enzyme release.

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Acid phosphatase has been localized by cytochemical techniques in aleurone layers of dry barley (Hordeum vulgare L.) grains, in imbibed half-grains and in isolated layers treated with and without gibberellic acid (GA3). A major fraction of the enzyme activity is located in the cell walls. During

Tannins as gibberellin antagonists in the synthesis of alpha-amylase and Acid phosphatase by barley seeds.

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The tannins chebulinic acid or tara tannin were added to an incubation system in which GA(3) induces enzyme synthesis in endosperm half seeds of barley (Hordeum vulgare L.). The activity of amylase and acid phosphatase in the incubation medium was reduced compared to the activity in the medium after

Regulation of the wheat MAP kinase phosphatase 1 by 14-3-3 proteins.

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Plant MAP kinase phosphatases (MKPs) are major regulators of MAPK signaling pathways and play crucial roles in controlling growth, development and stress responses. The presence of several functional domains in plant MKPs such as a dual specificity phosphatase catalytic domain, gelsolin,

Localization of gibberellic acid-induced acid phosphatase activity in the endoplasmic reticulum of barley aleurone cells with the electron microscope.

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A metal-salt precipitation method with p-nitrophenyl phosphate as substrate has been used to localize in the electron microscope acid phosphatase activity in isolated aleurone layers of barley (Hordeum vulgare L.), treated for 16 h in the presence or absence of gibberellic acid (GA3). The paper

Phosphatase activity in barley proteins tightly bound to DNA and its development-dependent changes.

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The tightly bound proteins (TBPs), a protein group that remains attached to DNA either covalently or noncovalently after deproteinization, have been found in numerous eukaryotic species. Some TBPs isolated from mammalian and yeast cells possess phosphatase or kinase activity. The aim of this study

Differential effect of gibberellic Acid on enhancement and release of Acid phosphatase in barley half-seeds.

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Acid phosphatase activity in half-seeds of a huskless barley (Hordeum vulgare L. cv. Ehimehadaka No. 1) increased linearly after a lag period of about 12 h. Gibberellic acid (GA(3)) lowered the acid phosphatase activity in half-seeds after about 12 h, while it increased the enzyme activity in the

Comparative phytohormone profiles, lipid kinase and lipid phosphatase activities in barley aleurone, coleoptile, and root tissues.

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We analyzed lipid kinase and lipid phosphatase activities and determined endogenous phytohormone levels by liquid chromatography-tandem mass spectrometry in root and coleoptile tissues following germination of barley (Hordeum vulgare) seeds. The enzymes showing highest activity in aleurone cells

Involvement of protein kinase and extraplastidic serine/threonine protein phosphatases in signaling pathways regulating plastid transcription and the psbD blue light-responsive promoter in barley.

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We investigated the signaling pathways that control changes in plastid transcription in response to development and light. Plastid gene expression was analyzed in dark-grown barley (Hordeum vulgare L.) seedlings treated in vivo with an inhibitor of protein phosphatases 1 and 2A, okadaic acid (OA),

Effect of vanadate on bean leaf movement, stomatal conductance, barley leaf unrolling, respiration, and phosphatase activity.

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Vanadate (Na(3) VO(4)) inhibits leaf movement and stomatal conductance of Phaseolus vulgaris L. cv. Carlos Favorit in light-dark cycles as well as photomorphogenetic leaf unrolling of Hordeum vulgare L. cv. Rupal. Inhibition was 50% by 10 to 100 micromolar vanadate and 100% by millimolar vanadate.

Cloning and characterization of purple acid phosphatase phytases from wheat, barley, maize, and rice.

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Barley (Hordeum vulgare) and wheat (Triticum aestivum) possess significant phytase activity in the mature grains. Maize (Zea mays) and rice (Oryza sativa) possess little or virtually no preformed phytase activity in the mature grain and depend fully on de novo synthesis during germination. Here, it

Sucrose-phosphatase gene families in plants.

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Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the final step in the pathway of sucrose biosynthesis and higher plants contain multiple isoforms of the enzyme encoded by different genes. The genome of the dicotyledonous plant Arabidopsis thaliana (thale cress) contains four SPP-like genes on

Characterization of a multifunctional inositol phosphate kinase from rice and barley belonging to the ATP-grasp superfamily.

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OsIpk and HvIpk, inositol phosphate kinases, were cloned from rice (Oryza sativa L. var. indica, IR64) and barley (Hordeum vulgare) respectively. Sequence alignment showed that they belong to the ATP-grasp family, which includes inositol 1,3,4-trisphosphate 5/6-kinase from humans and Arabidopsis.

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