vigna laurentii/phosphatase

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Immobilization of acid phosphatase from Vigna aconitifolia seeds on chitosan beads and its characterization.

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Acid phosphatase isolated from Vigna aconitifolia seeds was immobilized onto glutaraldehyde activated chitosan beads by crosslinking method. Chitosan beads activated with 2% of glutaraldehyde have demonstrated maximum immobilization yield (∼ 83%). The immobilized enzyme showed optimum activity at pH

Isolation and enzymatic properties of a nonspecific acid phosphatase from Vigna aconitifolia seeds.

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Acid phosphatase (EC 3.1.3.2) from Vigna aconitifolia seeds was purified to apparent homogeneity by using ammonium sulfate fractionation and cation-exchange chromatography [carboxymethyl (CM) cellulose]. The enzyme was 228-fold purified with 14.6% recovery. Analytical gel filtration chromatography

The inhibitory effect of metals and other ions on acid phosphatase activity from Vigna aconitifolia seeds.

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Sensitivity of acid phosphatase from Vigna aconitifolia seeds to metal ions, fluoride, and phosphate was examined. All the effectors had different degree of inhibitory effect on the enzyme. Among metal ions, molybdate and ferric ion were observed to be most potent inhibitors and both exhibited mixed

Effect of several germination treatments on phosphatases activities and degradation of phytate in faba bean (Vicia faba L.) and azuki bean (Vigna angularis L.).

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Two assays were conducted to investigate the changes of faba bean (Vicia faba L.) and azuki bean (Vigna angularis L.) phosphatases (phytase [Phy] and acid phosphatase [AcPh]) and the degradation of its substrates (inositol phosphate esters) during seed germination. The 1st assay was to establish the

Two novel plant cDNAs homologous to animal type-2 phosphatidate phosphatase are expressed in cowpea leaves and are differently regulated by water deficits.

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Two cDNAs encoding putative phosphatidate phosphatases (PAPs) designated VuPAP-alpha and VuPAP-beta were cloned in cowpea (Vigna unguiculata L.) leaves. The predicted proteins have six membrane-spanning regions in common with animal type-2 PAPs. Unlike VuPAP-beta, VuPAP-alpha has an N-terminal

Cloning and characterization of drought-stimulated phosphatidic acid phosphatase genes from Vigna unguiculata.

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Under environmental stresses, several lipolytic enzymes are known to be activated and to contribute to membrane lipid turnover and generation of second messengers. In animal cells, phosphatidic acid phosphatase (PAP, EC 3.1.3.4), which dephosphorylates phosphatidic acid generating diacylglycerol, is

Effects of nitrogen fertilization on soil nutrient concentration and phosphatase activity and forage nutrient uptake from a grazed pasture system.

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Over a 3-year period, the effect of differing N-application regimes on soil extractable-P concentration, soil phosphatase activity, and forage P uptake in a P-enriched grazed-pasture system was investigated. In the fall of each year, six 0.28-ha plots were overseeded with triticale ( × Triticosecale

Purification of acid phosphatase I from germinating seeds of Vigna sinensis.

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Acid phosphatase I (AP-I) is the major isoform of Vigna acid phosphatase. It is constitutively expressed in seed cotyledons during germination. AP-I was separated from other isoforms and purified to homogeneity by three simple purification steps; (NH4)2SO4 precipitation, and phosphocellulose and

Isolation and Characterization of Phosphoenolpyruvate Phosphatase from Germinating Mung Beans (Vigna radiata).

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A phosphoenolpyruvate (PEP) phosphatase was purified to homogeneity from germinating mung beans (Vigna radiata). It was found to be a tetrameric protein (molecular mass 240,000 daltons) made up of apparently identical subunits (subunit molecular mass 60,000 daltons). It was free from bound

Purification, characterisation and steady state kinetic properties of cytosolic pyruvate kinase free of phosphoenol pyruvate phosphatase activity from germinating mung beans (Vigna radiata L.)

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Mung bean pyruvate kinase (PK) practically free from PEP-phosphatase has been purified about 36 fold. The enzyme is irreversibly inactivated on desalting by gel filtration or dialysis (without EDTA). The inactivation is also observed in the presence of ATP, Mg2+ or thiols but is prevented by a

Acyl phosphatase of Vigna catjang.

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A pathway for photosynthetic carbon flow to mannitol in celery leaves : activity and localization of key enzymes.

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In the polyol producing plant, celery (Apium graveolens L.), mannitol is a major photosynthetic product and a form in which carbohydrate is translocated. Measurements of whole leaf extracts of celery indicated substantial activity of the following enzymes: mannose-6-P reductase, mannose-6-P

The role of VuMATE1 expression in aluminium-inducible citrate secretion in rice bean (Vigna umbellata) roots.

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Aluminium (Al)-activated citrate secretion plays an important role in Al resistance in a number of plant species, such as rice bean (Vigna umbellata). This study further characterized the regulation of VuMATE1, an aluminium-activated citrate transporter. Al stress induced VuMATE1 expression,

Regulation of the differentiation of osteoblasts and osteoclasts by a hot-water extract of adzuki beans (Vigna angularis).

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Osteoporosis is a global public health problem thought to be caused by an imbalance in bone metabolism. We examined in this study the 40% ethanol fraction of HP-20 resin in combination with a hot-water adzuki extract (EtEx.40) for its effect on osteoblast and osteoclast differentiation.

Peroxidases from an invasive Mesquite species for management and restoration of fertility of phenolic-contaminated soil.

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Phenolics drive the global economy, but they also pose threats to soil health and plant growth. Enzymes like peroxidase have the potential to remove the phenolic contaminants from the wastewater; however, their role in restoring soil health and improving plant growth has not yet been ascertained. We

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