spinacia spinosa/phosphatase

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Regulation of spinach SNF1-related (SnRK1) kinases by protein kinases and phosphatases is associated with phosphorylation of the T loop and is regulated by 5'-AMP.

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Members of the SNF1-related protein kinase-1 (SnRK1) subfamily of protein kinases are higher plant homologues of mammalian AMP-activated and yeast SNF1 protein kinases. Based on analogies with the mammalian system, we surmised that the SnRK1 kinases would be regulated by phosphorylation on a

Choline kinase and phosphorylcholine phosphatase in plants.

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Choline kinase was present in barley and wheat roots and leaves of barley, wheat, tobacco, spinach and squash plants. The kinase was purified 25-fold from spinach leaves. The enzyme had a broad pH optimum between 7.5 and 10.0. Mg(++) was required for activity and in the presence of Mg(++) the enzyme

Anion and divalent cation activation of phosphoglycolate phosphatase from leaves.

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Phosphoglycolate (P-glycolate) phosphatase was purified 223-fold from spinach leaves by (NH4)2SO4 fractionation, DEAE-cellulose chromatography, and Sephadex G-200 chromatography. The partially purified enzyme had a broad pH optimum between 5.6 and 8.0 and was specific for the hydrolysis of

Protein histidine phosphatase activity in rat liver and spinach leaves.

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Whole cell extracts from rat liver or spinach leaves contain divalent ion-independent protein histidine phosphatase activity due to phosphatases of the PP1/PP2A family. In the rat liver extract, almost all the activity was found in the PP1, PP2A1 and PP2A2 peaks. In the spinach leaf extract, four

The use of bacterial alkaline phosphatase assay for rapid monitoring of bacterial counts on spinach.

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This study was undertaken to evaluate the applicability of bacterial alkaline phosphatase (ALP) activity for rapid monitoring of total mesophilic bacteria counts in spinach. A set of fresh and decayed spinach mixtures were tested to rapidly (10 min) monitor spinach bacterial counts. To assay ALP

Sucrose-phosphate synthase phosphatase, a type 2A protein phosphatase, changes its sensitivity towards inhibition by inorganic phosphate in spinach leaves.

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The activity of a type 2A protein phosphatase from spinach leaves was monitored using phosphorylated sucrose-phosphate synthase (SPS) as a substrate. After partial purification the overall activities of sucrose-phosphate synthase phosphatase (SPS-P) recovered from leaves harvested in the dark and in

The action of phosphatidate phosphatase on the fatty-acid composition of safflower triacylglycerol and spinach glycerolipids.

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The microsomal phosphatidate phosphatase (EC 3.1.3.4) in maturing seeds of safflower (Carthamus tinctorius L.) was specific and selective for unsaturated phosphatidates. The relative order of specificity for phosphatidate molecular species was 1,2-dilinoleoyl = 1,2-dioleoyl > 1-palmitoyl-2-oleoyl >

Sucrose-phosphate synthase is dephosphorylated by protein phosphatase 2A in spinach leaves. Evidence from the effects of okadaic acid and microcystin.

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Sucrose-phosphate synthase (SPS) purified from spinach leaves harvested in the dark, was activated by mammalian protein phosphatase 2A (PP2A). Activation of SPS in a fraction from darkened spinach leaves was largely prevented by either okadaic acid or microcystin-LR (specific inhibitors of PPI and

Properties of a Membrane-bound Phosphatase from the Thylakoids of Spinach Chloroplasts.

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A 3-phosphoglycerate phosphatase activity of about 2 micromoles per minute per milligram chlorophyll is associated with the thylakoid membranes of spinach chloroplasts. The K(m) for 3-phosphoglycerate is 3 millimolar. The enzyme can be solubilized from thylakoid membranes by treatment with 0.33

Activation of sucrose-phosphate synthase from darkened spinach leaves by an endogenous protein phosphatase.

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Sucrose-phosphate synthase (SPS; EC 2.4.1.14) extracted from darkened spinach (Spinacia oleracea L.) leaves has a low activation state, defined as the ratio of activity measured with limiting substrates (plus the inhibitor Pi) to activity with saturating substrates (maximum velocity). Preincubation

Unexpected specificity in the thioredoxin activation of fructose-bis-phosphatases from different plants.

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Green seedlings of soy bean and wheat contain, like the plant seeds, multiple thioredoxin proteins which possess all typical thioredoxin properties but are inactive in the stimulation assay with spinach fructose-bis-phosphatase. However the pure proteins do have thioredoxin f activity when tested

Protein phosphatase 2A and its [3H]cantharidin/[3H]endothall thioanhydride binding site. Inhibitor specificity of cantharidin and ATP analogues.

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The target site for cantharidin (CA) and its analogues was isolated recently from mouse liver and identified as protein phosphatase (PP2A) in the heterodimeric form known as PP2A2. The most toxic CA analogue, endothall thioanhydride (ETA) (mouse i.p. LD50 0.3 mg/kg), appears to have the same binding

3-phosphoglycerate phosphatase activity in chloroplast preparations as a result of contamination by Acid phosphatase.

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The presence of a nonspecific acid phosphatase which had high activity with 3-phosphoglycerate as substrate has recently been reported in Spinacia oleracea L. chloroplasts (Mulligan, Tolbert 1980 Plant Physiol 66: 1169-1173). The subcellular localization of this activity has been reinvestigated by

3-Phosphoglycerate Phosphatase in Plants: III. Activity Associated with Starch Particles.

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A particulate form of 3-phosphoglycerate phosphatase represents about 20% of this activity in spinach (Spinacia oleracea var. Longstanding Bloomsdale) leaves. By differential and isopycnic sucrose density gradient centrifugation, all the particulate activity was found in starch grains that pelleted

Characterization of a phosphoenzyme intermediate in the reaction of phosphoglycolate phosphatase.

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When 32P-glycolate and phosphoglycolate phosphatase from spinach are mixed, 32P is incorporated into acid precipitated protein. Properties that relate the phosphorylation of the enzyme to the phosphatase are: the Km value for P-glycolate is similar for protein phosphorylation and substrate

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