linoleic-acid-hydroperoxide has been researched along with methyl-linoleate* in 2 studies
2 other study(ies) available for linoleic-acid-hydroperoxide and methyl-linoleate
Article | Year |
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Artifact formation during transmethylation of lipid peroxides.
By-product formation during base-catalyzed transesterification of lipid peroxides was observed in model experiments. A partially oxidized linoleic acid methyl ester as well as purified hydroxylinoleates served as test compounds. By-products formed during a simulated transmethylation of purified hydroxylinoleates were separated from the main components by means of thin-layer chromatography. The loss attributable to these by-products amounted to 10%. Oxygenated fatty acid derivatives were completely destroyed by acid-catalyzed transmethylation. Catalytic hydrogenation prior to base-catalyzed transmethylation proved to be a simple means to minimize side-product formation. By using this technique the yield of hydroxystearates from a partially autoxidized linoleic acid methyl ester preparation was improved significantly. Topics: Artifacts; Chromatography, Thin Layer; Gas Chromatography-Mass Spectrometry; Kinetics; Linoleic Acids; Lipid Peroxidation; Lipid Peroxides; Methylation; Oxidation-Reduction | 1992 |
Comparative studies on the effects of linoleate and methyl linoleate and their hydroperoxides on the respiration and reactivities of rat heart mitochondria.
Linoleate hydroperoxide and linoleate at concentrations of 100-140 nmol-mg protein activated state 4 respiration of rat heart mitochondria 4.2-fold, increased the apparent enthalpy change of the respiration per gram atom of oxygen consumed from -148 to -226 kJ/O and completely inhibited oxidative phosphorylation. Methyl linoleate hydroperoxide or methyl linoleate did not show the same effects. Further addition of linoleate hydroperoxide or linoleate induced oligomycin-insensitive Mg-ATPase to a level 5 or 2 times, respectively, that obtained with 120 muM dinitrophenol, accompanied by clearing of the mitochondrial suspension and release of malate dehydrogenase from the matrix. Methyl linoleate hydroperoxide had the same effects except that the induced Mg-ATPase activity retained oligomycin sensitivity. Methyl linoleate did not show either effect. Topics: Adenosine Triphosphatases; Animals; Calorimetry; Dose-Response Relationship, Drug; Enzyme Activation; Linoleic Acids; Lipid Peroxides; Magnesium; Male; Mitochondria, Heart; Oxidative Phosphorylation; Oxygen Consumption; Rats | 1980 |