OXIDATIVE INACTIVATION OF ANGIOTENSIN-CONVERTING ENZYMEстатья
Информация о цитировании статьи получена из
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 29 мая 2015 г.
Местоположение издательства:Road Town, United Kingdom
Первая страница:39
Последняя страница:44
Аннотация:Hydrogen peroxide in vitro inactivates isolated human angiotensin-converting enzyme (ACE), while the addition of catalase neutralizes this effect of H2O2. Lung and kidney ACE are equally sensitive to hydrogen peroxide. When oxidants (H2O2 or a mixture of H2O2/ascorbic acid and H2O2/Fe2+) are added to the membrane fraction or a lung homogenate inactivation of membrane-bound ACE is substantially less pronounced, despite the substantial accumulation of lipid peroxidation products. Pronounced inactivation of ACE in the membrane fraction (up to 55% of the initial activity) was observed when it was incubated with a mixture of glucose:glucose oxidase:Fe2+. Probably the oxidative potential of H2O2 in the tissue is expended primarily not on the inactivation of ACE but on the oxidation of other membrane components, for example, lipids.