phospholipase/potato

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Molecular and enzymatic characterization of three phosphoinositide-specific phospholipase C isoforms from potato.

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Many cellular responses to stimulation of cell-surface receptors by extracellular signals are transmitted across the plasma membrane by hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2), which is cleaved into diacylglycerol and inositol-1,4,5-trisphosphate by phosphoinositide-specific

Purification and characterization of an a type phospholipase from potato and its effect on potato mitochondria.

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A potato (Solanum tuberosum) phospholipid acyl-hydrolase, which - in the pH range 7.5 to 8.5-is at least 10,000 times more effective with phospholipids than with galactolipids, has been purified and characterized. It is a soluble enzyme readily distinguished from a neutral lipid lipase and a third

A cytosolic phospholipase A2 from potato tissues appears to be patatin.

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Phospholipase (PL) A2 is involved in signal transduction in the resistance reaction that is induced in potato by inoculation of an incompatible race of Phytophthora infestans, the late blight fungus, or by treatment with fungal elicitor hyphal wall components (Kawakita et al. 1993). In this study,

Cloning, expression, purification and characterization of patatin, a novel phospholipase A.

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Patatin is the major protein constituent of potato tubers and displays broad esterase activity. The native enzyme actually belongs to a highly homologous multigene family of vacuolar glycoproteins. From these, the patB2 patatin gene was selected and cloned into pUC19 without its signal sequence but

Potato tuber phospholipids contain colneleic acid in the 2-position.

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Colneleic acid (9-[1'(E),3'(Z)-nonadienyloxy]-8(E)-nonenoic acid) is produced from linoleic acid by the sequential action of 9-lipoxygenase and divinyl ether synthase. We demonstrate that a small fraction of the colneleic acid in potato tubers is esterified in phospholipids. This colneleic acid was

Purification and properties of a lipid acyl-hydrolase from potato tubers.

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1. A pure lipid acyl-hydrolase was prepared from potato tubers by acetone precipitation, Sephadex G-100 and DEAE-Sephadex A-50 column chromatography, and by electrofocusing. 2. The purified enzyme was an acidic protein of pI 5.0 and molecular weight of about 70 000. Km values were 0.38 mM for

Comparative Membrane-Associated Proteomics of Three Different Immune Reactions in Potato.

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Plants have evolved different types of immune reactions but large-scale proteomics about these processes are lacking, especially in the case of agriculturally important crop pathosystems. We have established a system for investigating PAMP-triggered immunity (PTI) and two different

Isolation and properties of lysosomes from dark-grown potato shoots.

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A method is described for the isolation of lysosomal fractions from dark-grown potato shoots using a single stage separation on a Ficoll gradient. Peaks of acid hydrolase activity consisting of acid phosphatase, phosphodiesterase, ribonuclease, carboxylic esterase and β-glycerophosphatase were well

Granulocyte-macrophage colony-stimulating factor (GM-CSF) promotes phosphorylation and an increase in the activity of cytosolic phospholipase A2 in human neutrophils.

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Incubation of human neutrophils with 500 pM granulocyte-macrophage colony-stimulating factor (GM-CSF) results in a rapid and time-dependent increase in the phosphorylation of cytosolic phospholipase A2 (cPLA2), which was reflected in a slower electrophoretic mobility of the enzyme. The

Pseudomonas aeruginosa causes acute lung injury via the catalytic activity of the patatin-like phospholipase domain of ExoU.

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OBJECTIVE Acute lung injury in Pseudomonas aeruginosa pneumonia depends primarily on ExoU toxin being delivered directly into the eukaryotic cell cytosol through the type III secretion system. The amino-acid sequence of ExoU has a potato patatin-like phospholipase domain, similar to the sequence of

Phytophthora infestans small phospholipase D-like proteins elicit plant cell death and promote virulence.

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The successful invasion of host tissue by (hemi-)biotrophic plant pathogens is dependent on modifications of the host plasma membrane to facilitate the two-way transfer of proteins and other compounds. Haustorium formation and the establishment of extrahaustorial membranes are probably dependent on

The existence of phospholipase A(2) activity in plant mitochondria and its activation by hyperosmotic stress in durum wheat (Triticum durum Desf.).

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The activity of mitochondrial phospholipase A(2) (PLA(2)) was shown for the first time in plants. It was observed in etiolated seedlings from durum wheat, barley, tomato, spelt and green seedlings of maize, but not in potato and topinambur tubers and lentil etiolated seedlings. This result was

Hispidospermidin, a novel phospholipase C inhibitor produced by Chaetosphaeronema hispidulum (Cda) Moesz NR 7127. I. Screening, taxonomy, and fermentation.

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A novel phospholipase C inhibitor, hispidospermidin, was discovered from a fungal culture broth. The producing fungus, NR 7127, formed abundant pycnidia on banana leaf agar under near UV light. The ostiolate pycnidia were dark colored with a short beak possessing numerous protruding setae. The

Regulation by Lipids of Plant Microsomal Enzymes: II. LIPID DEPENDENCE OF THE NADH-CYTOCHROME c REDUCTASE OF POTATO TUBERS.

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Microsomal membranes from potato tubers were treated with a phospholipase C extracted from Bacillus cereus. A positive correlation could be observed between the hydrolysis of membranous phospholipids and the decrease of the NADH-cytochrome c reductase activity. Addition of total lipid or

Purification and properties of a lipolytic acyl-hydrolase from potato leaves.

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A lipolytic acyl-hydrolase was purified 520-fold from an homogenate of potato leaves (Solanum tuberosum L. cv. Benimaru). The purified enzyme showed a single protein band on polyacrylamide gel electrophoresis. The enzyme had an isoelectric point of 4.6 and a molecular weight of about 110,000. It had

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