Hydrogen Peroxide Production by Rat Brain In Vivo
Hydrogen Peroxide Production by Rat Brain In Vivo
复制标题
大鼠脑体内产生过氧化氢
作者：
P. Sinet;R. Heikkila;G. Cohen
翻译后摘要：H2 O2的生产，通过大鼠大脑在体内观察与脑过氧化氢酶的测量的基础上的方法。对大鼠给予3-氨基-1，2，4-三唑（一种过氧化氢酶的H2 O2依赖性抑制剂），导致纹状体和前额叶皮质匀浆的上清液和沉淀组分中脑过氧化氢酶活性的进行性抑制。预防过氧化氢酶抑制的乙醇事先管理证实，过氧化氢酶抑制在体内依赖于H2 O2。大部分过氧化氢酶（30 - 33%）出现在慢速均质化程序的上清液部分中，未被红细胞或毛细血管显著污染。在整个匀浆中，不到6%的过氧化氢酶活性归因于红细胞。通过帕吉林或利血平修饰细胞内单胺氧化酶活性并没有改变氨基三唑对过氧化氢酶的抑制率。这些数据的一个可能的解释是，由线粒体单胺氧化酶产生的H2 O2没有达到过氧化氢酶室，过氧化氢酶包含在颗粒中描述的其他研究人员作为大脑的微过氧化物酶体。在体外研究中，证实了以多巴胺或5-羟色胺为底物的大鼠脑线粒体产生H2 O2。
Abstract: H2 O2 production by rat brain in vivo was observed with a method based on the measurement of brain catalase. The administration to the rat of 3‐amino‐1, 2, 4‐triazole, an H2 O2‐ dependent inhibitor of catalase, caused progressive inhibition of brain catalase activity in both the supernatant and pellet fractions of homogenates of the striatum and prefrontal cortex. The prevention of catalase inhibition by prior administration of ethanol confirmed that catalase inhibition in vivo was dependent upon H2 O2. A significant portion of the catalase (30‐33%) appeared in the supernatant fraction from a slow‐speed homogenization procedure and was not significantly contaminated by either erythrocytes or capillaries. In the whole homogenate, less than 6% of the catalase activity was attributed to erythrocytes. Modification of intracellular monoamine oxidase activity by either pargyline or reserpine did not change the rate of inhibition of catalase by aminotriazole. A probable interpretation of these data is that H2 O2 generated by mitochondrial monoamine oxidase does not reach the catalase compartment; the catalase is contained in particles described by other investigators as the microperoxisomes of brain. In studies in vitro, the production of H2 O2 by rat brain mitochondria with either dopamine or serotonin as substrate was confirmed.