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lipoxygenase/pomme de terre
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Immobilization of potato tuber lipoxygenase on oxirane acrylic beads.
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In this study, lipoxygenase from potato tuber has been purified by a method involving hydrophobic chromatography and the purified enzyme immobilized by covalent coupling to oxirane acrylic beads. The immobilized lipoxygenase exhibited increased long-term stability without a significant modification
Inhibition of phytoalexin synthesis in arachidonic Acid-stressed potato tissue by inhibitors of lipoxygenase and cyanide-resistant respiration.
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Arachidonic acid-stressed potato tuber discs synthesized the phytoalexin rishitin. This synthesis was inhibited by salicylhydroxamic acid (SHAM), and to a lesser extent by tetraethylthiuram disulfide (disulfiram). Disulfiram was less effective apparently because it was inactivated in the tuber
Antisense-mediated depletion of a potato lipoxygenase reduces wound induction of proteinase inhibitors and increases weight gain of insect pests.
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De novo jasmonic acid (JA) synthesis is required for wound-induced expression of proteinase inhibitors and other defense genes in potato and tomato. The first step in JA biosynthesis involves lipoxygenase (LOX) introducing molecular oxygen at the C-13 position of linolenic acid. We previously have
Inactivation of potato lipoxygenase by hydroperoxy acids as suicide substrates.
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The preincubation of potato lipoxygenase with 9(S)-hydroperoxyoctadecatrienoic acid, 15(S)-hydroperoxyeicosatetraenoic acid or 5(S)-hydroperoxyeicosatetraenoic acid which can be subjected to further lipoxygenation led to the gradual inactivation of the lipoxygenase activity, whereas
Stabilization of potato tuber lipoxygenase on talc.
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Potato tuber lipoxygenase, like many plant enzymes is a very labile protein and can lose activity during or after the purification procedure. In order to overcome this problem, we immobilized potato tuber lipoxygenase by adsorption on talc, a silicate support. Lipoxygenase adsorption greatly
Inhibition of potato lipoxygenase by linoleyl hydroxamic acid: kinetic and EPR spectral evidence for a two-step reaction.
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The reaction mechanism of an electrophoretically pure potato tuber lipoxygenase (ptLOX) was studied by EPR spectroscopy. An EPR spectrum of the 'native' ptLOX recorded at 4.5+/-0.5 K showed signals of a high-spin (pseudo) axial Fe(3+) with a g-value of approx. 6.3+/-0.1 with a shoulder at
Oxidation of linoleyl alcohol by potato tuber lipoxygenase: kinetics and positional, stereo, and geometrical (cis, trans) specificity of the reaction.
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The dioxygenation of linoleyl alcohol (LAL) by potato tuber lipoxygenase leads to formation of two positional isomeric products--9- and 13-hydroperoxyoctadecadien-1-ols (Butovich, I. A., Luk'yanova, S. M., and Reddy, C. C. (1998) Biochem. Biophys. Res. Commun. 249, 344-349). In the present study, we
Conversion of dihomo-gamma-linolenic acid to mono- and dihydroxy acids by potato lipoxygenase: evidence for the formation of 8,9-leukotriene A3.
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Evidence for the formation of a positional isomer of leukotriene (LT) C3 (8,9-LTC3) from dihomo-gamma-linolenic acid has been published (Hammarström, S. J. Biol. Chem. 256, 7712-7714, 1981). This report describes the conversion of dihomo-gamma-linolenic acid to a postulated intermediate in former
Oxidation of linoleyl alcohol by potato tuber lipoxygenase: possible mechanism and the role of carboxylic group in substrate binding.
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We have studied the aerobic oxidation of linoleyl alcohol (LAL) by potato tuber lipoxygenase in the presence of 0.02% (w/v) non-ionic detergent Lubrol PX (and its analog C12E10) and 0.1 mM sodium dodecyl sulfate to investigate the role of carboxylic group in substrate binding. While the enzyme
Double hydroperoxidation of alpha-linolenic acid by potato tuber lipoxygenase.
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The potato tuber lipoxygenase preparations convert alpha-linolenic acid not only to 9(S)-HPOTE, but also to some more polar metabolites. Two of these polar products, I and II, with ultraviolet absorbance maxima at 267 nm were purified by HPLC. It was found that metabolites I and II have,
The unusual action of (R,S)-2-hydroxy-2-trifluoromethyl-trans-n-octadec-4-enoic acid on 5-lipoxygenase from potato tubers.
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We found that (R,S)-2-hydroxy-2-trifluoromethyl-trans-n-octadec-4-enoic acid (HTFOA) is a powerful activator of 5-lipoxygenase from potato tubers. The degree of activation of the enzyme is proportional to the HTFOA concentration and is a maximum at about 0.1 mM independently of initial substrate
Transformation of 15-hydroperoxide of eicosapentaenoic acid to lipoxins and trihydroxyeicosatetraenoic acids by 5-lipoxygenase partially purified from potato tubers.
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Incubation of 15-hydroperoxide of 5,8,11,14,17-eicosapentaenoic acid (15-HPEPE) with 5-lipoxygenase enzyme, partially purified from potato tubers, resulted in the generation of 6 isomers of lipoxin A5. These compounds were identified by GC/MS analysis of their methyl ester and trimethylsilyl ether
Differential distribution of the lipoxygenase pathway enzymes within potato chloroplasts.
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The lipoxygenase pathway is responsible for the production of oxylipins, which are important compounds for plant defence responses. Jasmonic acid, the final product of the allene oxide synthase/allene oxide cyclase branch of the pathway, regulates wound-induced gene expression. In contrast, C6
[Thermoinactivation of potato 5-lipoxygenase and effect of phosphatidic acid on activation energy of denaturation].
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The investigation aim was to establish the structural-functional relations of individual lipid metabolism components: enzymes--lipoxygenases and membrane phospholipids. Influence of phosphatidic acid (PA)--allosteric activator of potato tuber 5-lipoxygenase (5-LO)--on thermoinactivation
Enzyme-catalyzed and enzyme-triggered pathways in dioxygenation of 1-monolinoleoyl-rac-glycerol by potato tuber lipoxygenase.
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It was shown for the first time that potato tuber lipoxygenase (ptLOX) catalyzed the aerobic oxidation of 1-monolinoleoyl-rac-glycerol (mLG) in a mixed micellar reaction solution with the non-ionic detergent monododecyl ether of decaoxyethylene glycol. No hydrolysis of mLG occurred during the
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