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脂氧合酶的氢过氧化物酶活性:过氧化氢依赖的外源化合物氧化作用。

Hydroperoxidase activity of lipoxygenase: hydrogen peroxide-dependent oxidation of xenobiotics.

作者信息

Kulkarni A P, Cook D C

机构信息

Department of Environmental and Occupational Health, College of Public Health, University of South Florida, Tampa 33612-3899.

出版信息

Biochem Biophys Res Commun. 1988 Sep 15;155(2):1075-81. doi: 10.1016/s0006-291x(88)80606-5.

Abstract

Since H2O2 is one of the major biologically available peroxides, its ability to support hydroperoxidase activity of highly purified soybean lipoxygenase was examined by monitoring co-oxidation of selected xenobiotics. All of the eight chemicals tested were found to be oxidized in the presence of H2O2. Tetramethylbenzidine oxidation was completely inhibited by the classical lipoxygenase inhibitor nordihydroguaiaretic acid. The reaction was enzymatic in nature and exhibited a acidic pH optimum. The data clearly indicate, for the first time, that H2O2 can efficiently replace fatty acid hydroperoxide in a xenobiotic oxidation reaction medicated by the hydroperoxidase activity of lipoxygenase.

摘要

由于过氧化氢是主要的生物可利用过氧化物之一,通过监测特定异生物质的共氧化作用,研究了其支持高度纯化的大豆脂氧合酶氢过氧化物酶活性的能力。所测试的八种化学物质在过氧化氢存在下均被氧化。四甲基联苯胺的氧化被经典的脂氧合酶抑制剂去甲二氢愈创木酸完全抑制。该反应本质上是酶促反应,最适pH呈酸性。这些数据首次清楚地表明,在由脂氧合酶的氢过氧化物酶活性介导的异生物质氧化反应中,过氧化氢能够有效地替代脂肪酸氢过氧化物。

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