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SUBUNIT SEPARATION IN REVERSED MICELLE SYSTEM REVEALS THE EXISTENCE OF ACTIVE-CENTERS BOTH ON LIGHT AND HEAVY GAMMA-GLUTAMYL-TRANSFERASE SUBUNITSстатья
Информация о цитировании статьи получена из
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Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: KABANOV AV, NAMETKIN SN, CHERNOV NN, KLYACHKO NL, LEVASHOV AV
- Журнал: FEBS Letters
- Том: 295
- Номер: 1-3
- Год издания: 1991
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 73
- Последняя страница: 76
- DOI: 10.1016/0014-5793(91)81388-O
- Аннотация: Regulation of supra-macromolecular composition and catalytic activity of a heterodimeric enzyme, gamma-glutamyltransferase, in the system of Aerosol OT (sodium bis(2-ethylhexyl) sulfosuccinate) reversed micelles in octane were studied. Variation of the surfactant hydration degree (parameter, determining dimensions of the polar inner cavity of the micelle) causes a reversible dissociation of the enzyme to light and heavy subunits. Both enzyme subunits possess catalytic activity. The light and heavy subunits of the enzyme were separated on a preparative scale in a reversed micelle system using ultracentrifugation. The active centers of gamma-glutamyltransferase were studied using its irreversible inhibitor -AT-125 (L-(alpha-S,5S)-alpha-amino-3-chloro-4, 5-dihydro-5-isoxazoleacetic acid). Separation of the gamma-glutamyltransferase subunits results in the 'opening' of a new active center located at the heavy subunit. In the dimer form of the enzyme this center is masked and it is not accessible to both substrate and inhibitor molecules.
- Добавил в систему: Клячко Наталья Львовна