Byczkowski J Z, Ramgoolie P J, Kulkarni A P
Toxicology Program, College of Public Health, University of South Florida, Tampa 33612.
Biochem Int. 1991 Nov;25(4):639-46.
The lipoxygenase-catalyzed hydroxylation of proline was studied in vitro in the presence of linoleic acid. The rate of reaction exhibited dependence on the concentration of proline, linoleic acid and the enzyme. The magnitude of hydroxyproline formed per mg of protein was time-dependent. Nordihydroguaiaretic acid at 0.1 mM concentration completely inhibited this reaction. No proline hydroxylation was detected during peroxidation of linoleic acid by vanadyl(IV). It is suggested that free-radical products of linoleic acid peroxidation may co-oxygenate proline in the presence of lipoxygenase.
在亚油酸存在的条件下，对脯氨酸的脂氧合酶催化羟基化反应进行了体外研究。反应速率表现出对脯氨酸、亚油酸和酶浓度的依赖性。每毫克蛋白质形成的羟脯氨酸量与时间有关。浓度为0.1 mM的去甲二氢愈创木酸完全抑制了该反应。在用氧钒（IV）使亚油酸过氧化的过程中未检测到脯氨酸羟基化。这表明在脂氧合酶存在的情况下，亚油酸过氧化产生的自由基产物可能会使脯氨酸发生共氧化。
