Sakharov I Iu, Dukhanina E A, Puchnina E A, Danilov S M, Muzykantov V R
Biokhimiia. 1991 Jan;56(1):55-62.
Hydrogen peroxide inactivates the purified human angiotensin-converting enzyme (ACE) in vitro; the inactivating effect of H2O2 is eliminated by an addition of catalase. The lung and kidney ACE are equally sensitive to the effect of hydrogen peroxide. After addition of oxidants (H2O2 alone or H2O2 + ascorbate or H2O2 + Fe2+ mixtures) to the membranes or homogenates of the lung, the inactivation of membrane-bound ACE is far less pronounced despite the large-scale accumulation of lipid peroxidation products. The marked inactivation of ACE in the membrane fraction (up to 55% of original activity) was observed during ACE incubation with a glucose:glucose oxidase:Fe2+ mixture. Presumably the oxidative potential of H2O2 in tissues in consumed, predominantly, for the oxidation of other components of the membrane (e.g., lipids) rather than for ACE inactivation.
过氧化氢在体外可使纯化的人血管紧张素转换酶（ACE）失活；添加过氧化氢酶可消除H2O2的失活作用。肺和肾中的ACE对过氧化氢的作用同样敏感。向肺的膜或匀浆中添加氧化剂（单独的H2O2或H2O2 +抗坏血酸或H2O2 + Fe2+混合物）后，尽管脂质过氧化产物大量积累，但膜结合ACE的失活并不明显。在ACE与葡萄糖：葡萄糖氧化酶：Fe2+混合物孵育期间，观察到膜组分中ACE有明显失活（高达原始活性的55%）。据推测，组织中H2O2的氧化电位主要用于膜的其他成分（如脂质）的氧化，而非ACE的失活。
