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[Different domain organization of two main conformational states of Na+/K+-ATPase]статья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 4 февраля 2014 г.
- Авторы: Petrushanko I.I.u, Mit’kevich V.A., Borzova V.A., Iakushev S.S., Lopina O.D., Makarov A.A.
- Журнал: Biophysics
- Том: 54
- Номер: 6
- Год издания: 2009
- Издательство: Maik Nauka/Interperiodica Publishing
- Местоположение издательства: Russian Federation
- Первая страница: 1019
- Последняя страница: 1025
- Аннотация: Na+/K+-ATPase generates an electrochemical gradient of Na+ and K+, which is necessary for the functioning of animal cells. During the catalytic act, the enzyme passes through two ground conformational states, E1 and E2. To characterize the domain organization of the protein in these conformations, the thermal denaturation of Na+/K+-ATPase from duck salt glands and rabbit kidneys has been studied in the presence of Na+ and K+, which induce the transition of the enzyme to the conformation E1 or E2. The melting curves for the apoforms of Na+/K+-ATPases have different shapes: the curve for the enzyme from the rabbit shows one transition at 56.1 degrees C, whereas the denaturation of Na+/K+-ATPase from the duck is characterized by two transitions, at 49.8 and 56.9 degrees C. Sodium and potassium ions abolish the difference in the domain organization of Na+/K+-ATPases. The melting curves for Na+/K+-ATPases in conformation E2 in both cases exhibit a single peak of thermal absorption at about 63 degrees C. The melting curves for the enzymes in conformation E1 show three peaks of thermal absorption, indicating the denaturation of three domains. The difference in the domain organization of Na+/K+-ATPase in conformations E1 and E2 may be of importance in different sensitivity of these conformations of the enzyme to temperature, proteolytic enzymes, and oxidative stress.
- Добавил в систему: Лопина Ольга Дмитриевна