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arachis hypogaea/phosphatase
L'enllaç es desa al porta-retalls
Pàgina 1 des de 26 resultats
Purification, kinetic properties and physicochemical characterization of a novel acid phosphatase (AP) from germinating peanut (Arachis hypogaea) seed.
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Acid phosphatase activity was detected in peanut (Arachis hypogaea) cotyledons during germination. Four (4) to six (6) days of germination was the meantime corresponding to maximum hydrolytic activity of this enzyme. The understanding of the role of acid phosphatase activity during germination led
Purification and characterization of an acid phosphatase from Arachis hypogaea.
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An acid phosphatase from Arachis hypogaea (peanuts) has been purified. The electrophoretically homogeneous enzyme preparation is free of any phophodiesterase activity. The enzyme has a molecular weight of 120,000. Among the various phosphomonoesters tested, p-nitrophenylphosphate was found to be its
[Activity of acid and alkaline phosphatases (intracellular and extracellular) in rhyzosphere fungi from Arachis hypogaea (Papiloneaceae)].
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The potential role of the fungi, isolated from the peanut rhizosphere, in the production of extracellular and intracellular acid and alkaline phosphatase, was evaluated in vitro. Acid and alkaline extracellular phosphatases showed the highest activities, and the Penicillium species were the most
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
In vitro screening for protein tyrosine phosphatase 1B and dipeptidyl peptidase IV inhibitors from selected Nigerian medicinal plants.
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OBJECTIVE
Protein tyrosine phosphatase 1B (PTP 1B) and dipeptidyl peptidase IV (DPP IV) have been identified as one of the drug targets for the treatment of Type-2 diabetes. This study was designed to screen for PTP 1B and DPP-IV inhibitors from some Nigerian medicinal plants.
METHODS
PTP 1B and
Influence of tebuconazole and copper hydroxide on phosphatase and urease activities in red sandy loam and black clay soils.
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The efficacy of two selected fungicides i.e., tebuconazole and coppoer hydroxide, was conducted experiments in laboratory and copper hydroxide on the two specific enzymes phosphatase and urease were determined in two different soil samples (red sandy loam and black clay soils) of groundnut (Arachis
Effect of insecticides alone and in combination with fungicides on nitrification and phosphatase activity in two groundnut (Arachis hypogeae L.) soils.
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The effect of selected pesticides, monocrotophos, chlorpyrifos alone and in combination with mancozeb and carbendazim, respectively, was tested on nitrification and phosphatase activity in two groundnut (Arachis hypogeae L.) soils. The oxidation of ammonical nitrogen was significantly enhanced under
Influence of selected insecticides on phosphatase activity in groundnut (Arachis hypogeae L.) soils.
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Selected insecticides, Chloropyrifos, Dichlorovos, Methyl parathion, Phorate and Methomyl, at concentrations ranging from 0 to 10 kg ha(-1) were tested for their non-target effects towards activity of phosphatases in two soils. In soil samples receiving 2.5 kg ha(-1) of the insecticides Dichlorovos,
Immobilization of acid phosphatase from arachis hypogaea on CM-cellulose.
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Influence of Salt Stress on Growth of Spermosphere Bacterial Communities in Different Peanut (Arachis hypogaea L.) Cultivars.
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BACKGROUND
Exposure of seeds to high salinity can cause reduced germination and poor seedling establishment. Improving the salt tolerance of peanut (Arachis hypogaea L.) seeds during germination is an important breeding goal of the peanut industry. Bacterial communities in[Lectins as reagents for the differentiation of serum enzymes. Lectins as reagents, I. (author's transl)].
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Lectins from Canavalia ensiformis, Phaseolus vulgaris, and Triticum vulgare react with arylamidase, alkaline phosphatase, gamma-glutamyltransferase, and cholinesterase of human sera by formation of enzymatically active, mostly insoluble complexes. Arylamidase, alkaline phosphatase, and
[Catalytic concentration, multiple forms, and lectin affinity of microsomal enzymes from human tissues: lectins as reagents, II (author's transl)].
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We estimated the concentrations, multiple forms, and lectin binding of five microsomal enzymes in particle free extracts from human kidney, pancreas, jejunal mucosa, and normal and cancerous liver. While arylesterase markedly reacted only with concanavalin A, arylamidase, alkaline phosphatase,
Galectin-1-mediated cell adhesion, invasion and cell death in human anaplastic large cell lymphoma: regulatory roles of cell surface glycans.
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Galectin-1 is known to be one of the extracellular matrix proteins. To elucidate the biological roles of galectin-1 in cell adhesion and invasion of human anaplastic large cell lymphoma, we performed cell adhesion and invasion assays using the anaplastic large cell lymphoma cell line H-ALCL, which
Peanut agglutinin (lectin from Arachis hypogaea) binding to hemopoietic cells: an immunophenotypic study using a biotin streptavidin technique.
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The lectin peanut agglutinin (PNA) was used to study the surface carbohydrate expression of galactose beta 1, 3, N-acetylgalactosamine by normal and malignant hemopoietic cells. Immunostaining was performed using biotinylated PNA and a streptavidin-alkaline phosphatase staining technique on 78
Biofunctional soyasaponin Bb in peanut (Arachis hypogaea L.) sprouts enhances bone morphogenetic protein-2-dependent osteogenic differentiation via activation of runt-related transcription factor 2 in C2C12 cells.
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Improvement of bone formation is necessary for successful treatment of the bone defects associated with osteoporosis. In this study, we sought to elucidate the osteogenic activity of peanut sprouts and their bioactive components. We found that peanut sprout water extract (PSWE) enhanced bone
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