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cotyledon/phosphatase

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DIFFERENTIAL ACTIVITIES OF ACID PHOSPHATASE FROM ADAXIAL AND ABAXIAL REGIONS OF LUPINUS LUTEUS (FABACEAE) COTYLEDONS.

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Acid phosphatases of abaxial and adaxial regions in the cotyledons of the Lupinus luteus which possess structurally distinct protein bodies were examined. Acid phosphatase activity was investigated by enzyme assays and by gel electrophoresis and was localized by cytochemical methods in the

Purification and characterization of acid phosphatase from cotyledons of germinating soybean seeds.

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Soybean acid phosphatase (orthophosphoric-monoester phosphohydrolase, EC 3.1.3.2) was completely separated from phytase (EC 3.1.3.8) isolated from cotyledons of germinating seeds and purified to homogeneity. A four-step purification regimen consisting of ammonium sulfate fractionation, and

Isolation of lysophosphatidic acid phosphatase from developing peanut cotyledons.

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The soluble fraction of immature peanut (Arachis hypogaea) was capable of dephosphorylating [(3)H]lysophosphatidic acid (LPA) to generate monoacylglycerol (MAG). The enzyme responsible for the generation of MAG, LPA phosphatase, has been identified in plants and purified by successive chromatography
Mixed micelles of (32)P-labeled phosphatidylcholine or phosphatidic acid (PA) and the nonionic detergent octylphenol polyethylene oxide (NP-40 Nonidet) were used to assay the activities of phospholipase D and PA phosphatase in crude extracts of mung bean (Vigna radiata) cotyledons. Together these
Phytic acid (myo-inositol hexakisphosphate) is the major storage form of phosphorus in plant seeds. During germination, stored reserves are used as a source of nutrients by the plant seedling. Phytic acid is degraded by the activity of phytases to yield inositol and free phosphate. Due to the lack

Acid phosphatase and ribonuclease in the cotyledons of germinating peas.

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The occurrence of a soluble glucose 6-phosphatase in cotyledon tissue of Phaseolus vulgaris during germination.

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Solubilization, purification and characterization of an acid phosphatase from the plasma membranes of peanut cotyledons.

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Glucose-6-phosphatase activity in a soluble fraction from cotyledon tissue of Brassica nigra.

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The timing of changes in total nitrogen and soluble amino nitrogen content, and in the activities of proteinase (pH 7.0), isocitrate lyase, catalase, phytase, phosphatase (pH 5.0), α-galactosidase and β-mannosidase were studied in extracts from the cotyledons, axis and endosperms of germinating and

Calcium- and calmodulin-regulated breakdown of phospholipid by microsomal membranes from bean cotyledons.

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Evidence for the involvement of Ca(2+) and calmodulin in the regulation of phospholipid breakdown by microsomal membranes from bean cotyledons has been obtained by following the formation of radiolabeled degradation products from [U-(14)C]phosphatidylcholine. Three membrane-associated enzymes were

The localization of enzymes in the cotyledons of Pisum arvense L. during germination.

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Enzyme activity is not uniformly distributed through the cotyledon of Pisum arvense. Initially the peripheral region, certain scattered cells of the storage tissue and the procambium show a high level of activity of succinic dehydrogenase, cytochrome oxidase, acid phosphatase and esterase. Activity

Isolation of a gene, PnFL-1, expressed in Pharbitis cotyledons during floral induction.

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A novel gene, designated PnFL-1, was isolated from flower-induced cotyledons in a short-day plant, Pharbitis nil, using messenger RNA differential display. PnFL-1 has no similarity to genes with known functions in databases, but the deduced amino acid sequence of the gene has 58% homology with a
Vein patterns in leaves and cotyledons form in a spatially regulated manner through the progressive recruitment of ground cells into vascular cell fate. To gain insight into venation patterning mechanisms, we have characterized the cotyledon vascular pattern2 (cvp2) mutants, which exhibit an

Purification of apyrase from yellow lupin cotyledons after extraction with perchloric acid.

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Neutralized 1 M perchloric acid (PCA) extracts of yellow lupin (Lupinus luteus) seedling cotyledons contain considerable amounts of apyrase (EC 3.6.1.5). Investigators who use PCA extraction for the estimation of nucleotide levels, particularly in plant tissues, should be aware of this danger. Only
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