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- W2052119046 abstract "Abstract A flavoprotein-oxidase isolated from pig hepatic microsomes catalyzes the NADPH- and oxygen-dependent N -oxidation of a variety of lipid-soluble sec - and tert -amines. The sec -amines are oxidized to the hydroxylamines; and the tert -amines, to the amine oxides. With one or two exceptions the isolated oxidase does not catalyze the oxidation of primary amines. However, primary alkylamines added to the reaction vessel increase the sec - and tert -amine N -oxidase activity of both the isolated enzyme and microsomes. The isolated oxidase contains 14 nmoles FAD and about 0.02 mg lipid/mg protein. The oxidase appears to be free from cytochromes but is contaminated with very small, but detectable, amounts of a hemoprotein that corresponds to catalase, both spectrally and in enzymic properties. The isolated enzyme is free from NADPH-cyt. c reductase, diaphorase, and monoamine oxidase activities." @default.
- W2052119046 created "2016-06-24" @default.
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- W2052119046 date "1972-05-01" @default.
- W2052119046 modified "2023-10-13" @default.
- W2052119046 title "Microsomal oxidase IV: Properties of a mixed-function amine oxidase isolated from pig liver microsomes" @default.
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- W2052119046 doi "https://doi.org/10.1016/0003-9861(72)90017-3" @default.
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