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- W1521197013 endingPage "965" @default.
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- W1521197013 abstract "Lipoxin B 4 (LXB 4 ) is metabolized to 20‐hydroxy‐LXB 4 by rat liver microsomes. The ω‐hydroxylation requires both molecular oxygen and NADPH, and is inhibited by carbon monoxide, indicating involvement of a cytochrome P ‐450 ( P ‐450). This is supported by inhibition of the reaction by antibodies raised against NADPH– P ‐450 reductase. The P ‐450 appears to be the one responsible for leukotriene B 4 ω‐hydroxylation, because leukotriene B 4 inhibits the formation of 20‐hydroxy‐LXB 4 and LXB 4 blocks the leukotriene B 4 ω‐hydroxylase activity in microsomes. Incubation of 20‐hydroxy‐LXB 4 with both rat liver cytosol and NAD + leads to formation of a more polar metabolite on high‐performance liquid chromatography. The metabolite is identified as 20‐carboxy‐LXB 4 , a novel metabolite of LXB 4 , based on analyses by ultraviolet spectrometry and by gas chromatography/mass spectrometry. The 20‐carboxy‐LXB 4 ‐forming activity is localized in cytosol, with an optimal pH of 8.5. The activity is dependent on NAD + , but NADP + can not replace NAD + . The reaction is inhibited by pyrazole and 4‐methylpyrazole, inhibitors of alcohol dehydrogenase, and by substrates of the enzyme such as ethanol and 20‐hydroxy‐leukotriene B 4 . Disulfiram, an inhibitor of aldehyde dehydrogenase, also blocks the 20‐carboxy‐LXB 4 formation. These observations suggest that both alcohol dehydrogenase and aldehyde dehydrogenase participate in the oxidation of 20‐hydroxy‐LXB 4 to 20‐carboxy‐LXB 4 ." @default.
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- W1521197013 date "1994-09-01" @default.
- W1521197013 modified "2023-10-07" @default.
- W1521197013 title "omega-Oxidation of Lipoxin B4 by Rat Liver. Identification of an omega-Carboxy Metabolite of Lipoxin B4" @default.
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- W1521197013 doi "https://doi.org/10.1111/j.1432-1033.1994.00959.x" @default.
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