|
ИСТИНА |
Войти в систему Регистрация |
ИПМех РАН |
||
Substrate-dependent inactivation of muscle pyruvate dehydrogenase: identification of the acetyl-substituted enzyme formстатья
Информация о цитировании статьи получена из
Scopus
Дата последнего поиска статьи во внешних источниках: 18 декабря 2013 г.
- Авторы: Khailova LS, Alexandrovitch OV, Severin SE
- Журнал: Biochemstry International
- Том: 10
- Номер: 2
- Год издания: 1985
- Первая страница: 291
- Последняя страница: 300
- Аннотация: The properties of the pyruvate dehydrogenase component isolated from the pigeon breast muscle pyruvate dehydrogenase complex were studied upon inactivation of the enzyme in an incomplete reaction mixture: in the presence of cofactors and pyruvate, and in the absence of electron acceptors. The substrate-dependent inactivation was shown to result in the modification of two sulfhydryl groups per mole of the enzyme, in the appearance of a maximum at 235 nm in the protein absorption spectrum, and in the involvement of 1.5 moles of the [2-14C]-pyruvate fragment per mole of the pyruvate dehydrogenase. The fragment-protein bond is acid-stable, labile in alkali, and breaks up in the presence of performic acid, neutral hydroxylamine and dithiothreitol. An acetyl-substituted form of pyruvate dehydrogenase appearing with the participation of sulfhydryl enzyme groups is suggested.
- Добавил в систему: Хайлова Людмила Самуиловна