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phospholipase d/mayi

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Phospholipase D (PLD) was purified to high homogeneity from rice bran (Oryza sativa L.). Two peaks of PLD activity were resolved by Mono Q anion-exchange chromatography. The molecular mass of PLD in both peaks was 82 kDa on SDS-PAGE and 78 kDa in gel filtration. Antibodies raised against the protein
N-acylethanolamines (NAEs) are lipid signaling mediators, which can be synthesized from dietary fatty acids via n-acylphosphatidylethanolamine-phospholipase D (NAPE-PLD) and in turn influence physiological outcomes; however, the roles of NAPE-PLD upon dietary fatty acid modulation are not fully

Effect of processing conditions on phospholipase D activity of corn kernel subcellular fractions.

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The influence of physicochemical conditions on the phospholipase D (PLD) activity of subcellular preparations of sweet corn (Zea mays L. cv. Peaches and Cream) kernels has been studied. The microsomal, mitochondrial, and cytosolic preparations of corn kernels possessed PLD activity albeit at varying

Evidence for and subcellular localization of a ca-stimulated phospholipase d from maize roots.

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Autolytic lipid changes in corn (Zea mays L.) root crude homogenates and isolated membranes were examined by the use of high performance thin-layer chromatography. In the absence of added CaCl(2), losses in phosphatidylcholine and other phospholipids corresponds to increase in fatty acids without
Nitric oxide (NO), an endogenous signaling molecule in animals and plants, mediates responses to abiotic and biotic stresses. Our previous work demonstrated that 100 microM sodium nitroprusside (SNP, an NO donor) treatment of maize seedlings increased K(+) accumulation in roots, leaves and sheathes,
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