13-hydroperoxylinoleic-acid and 15-hydroperoxy-5-8-11-13-eicosatetraenoic-acid

Linoleic acid-derived radicals, which are formed in the reaction of linoleic acid with soybean lipoxygenase, were trapped with nitrosobenzene and the resulting radical adducts were analysed by h.p.l.c.-e.p.r. and liquid chromatography-thermospray-m.s. Three nitrosobenzene radical adducts (peaks I, II and III) were detected; these gave the following parent ion masses: 402 for peak I, 402 for peak II, and 386 for peak III. The masses of peaks I and II correspond to the linoleic acid radicals with one more oxygen atom [L(O).]. The radicals are probably carbon-centred, because the use of 17O2 did not result in an additional hyperfine splitting. Computer simulation of the peak I radical adduct e.p.r. spectrum also suggested that the radical is carbon-centred. The peak I radical was also detected in the reaction of 13-hydroperoxylinoleic acid with FeSO4. From the above results, peak I is probably the 12,13-epoxylinoleic acid radical. An h.p.l.c.-e.p.r. experiment using [9,10,12,13-2H4]linoleic acid suggested that the 12,13-epoxylinoleic acid radical is a C-9-centred radical. Peak II is possibly an isomer of peak I. Peak III, which was observed in the reaction mixture without soybean lipoxygenase, corresponds to a linoleic acid radical (L.). The 12,13-epoxylinoleic acid radical, 12,13-epoxylinolenic acid radical and 14,15-epoxyarachidonic acid radical were also detected in the reactions of linoleic acid, linolenic acid and arachidonic acid respectively, with soybean lipoxygenase using nitrosobenzene and 2-methyl-2-nitrosopropane as spin-trapping agents.

Topics: Chromatography, High Pressure Liquid; Chromatography, Liquid; Electron Spin Resonance Spectroscopy; Free Radicals; Leukotrienes; Linoleic Acids; Linolenic Acids; Lipid Peroxides; Mass Spectrometry; Molecular Structure; Nitroso Compounds; Spin Labels; Structure-Activity Relationship

Fe(III)-bleomycin catalyzes the decomposition of 13-hydroperoxylinoleic acid and of 15-hydroperoxyarachidonic acid to produce small quantities of singlet oxygen. No singlet oxygen is produced when hydrogen peroxide, ethyl hydroperoxide, cumene hydroperoxide, and t-butyl hydroperoxide are used as substrates. The heme-containing catalysts, methemoglobin and hematin, have identical hydroperoxide substrate requirements for singlet oxygen production. The hydroperoxide requirements for singlet oxygen production correlate with those reported by Dix et al. (Dix, T.A., Fontana, R., Panthani, A., and Marnett, L.J. (1985) J. Biol. Chem. 260, 5358-5365) for the production of peroxyl radicals in the hematin-catalyzed decomposition of hydroperoxides. The bimolecular reaction of peroxyl radicals is a plausible reaction mechanism for the singlet oxygen production in the systems studied.

Topics: Arachidonic Acids; Bleomycin; Hydrogen Peroxide; Kinetics; Leukotrienes; Linoleic Acids; Lipid Peroxides; Luminescent Measurements; Methemoglobin; Oxygen; Peroxides; Photochemistry; Singlet Oxygen

Topics: Animals; Arachidonic Acid; Arachidonic Acids; Arteries; Dogs; Female; In Vitro Techniques; Indomethacin; Leukotrienes; Linoleic Acids; Lipid Peroxides; Male; Muscle Contraction; Muscle, Smooth, Vascular; Peroxides