STUDY OF ROTATIONAL MOBILITY OF MEMBRANE-BOUND NA,K-ATPASEстатья
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Web of Science
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Дата последнего поиска статьи во внешних источниках: 27 мая 2015 г.
Местоположение издательства:Road Town, United Kingdom
Первая страница:1425
Последняя страница:1431
Аннотация:The rotational mobility of the E(1) and E(2) conformers of duck salt gland Na,K-ATPase labelled with eosine-5'-isothiocyanate (EITC) was studied by measuring time-resolved phosphorescence anisotropy. Two types of rotational mobility were found for each conformer. The faster component with rotational correlation time of about 15 mu sec at 20 degrees C for both enzyme conformers is ascribed to the rotation of the (alpha beta)-protomer on the basis of the calculated apparent rotation radius. The slow component, whose rotational correlation time was 100-500 mu sec depending on experimental conditions, is suggested to reflect the presence of membrane associates formed by Na,K-ATPase protomers with each other or with other protein constituents. Increasing temperature tends to decrease the fast and increase the slower component of the phosphorescence anisotropy curve, which can be explained by association of protomers into oligomers of higher molecular mass. Their size depends on temperature and pH and may correspond to octamers under the most favorable conditions.