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Melittin induces both time-dependent aggregation and inhibition of Na,K-ATPase from duck salt glands however these two processes appear to occur independentlyстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Shorina E.A., Dolgova N.V., Rubtsov A.M., Storey K.B., Lopina O.D.
- Журнал: Biochimica et Biophysica Acta - Biomembranes
- Том: 1661
- Номер: 2
- Год издания: 2004
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 188
- Последняя страница: 195
- DOI: 10.1016/j.bbamem.2004.01.003
- Аннотация: Using cupric phenanthroline as a cross-linking agent, we have shown that melittin induced time-dependent aggregations of Na,K-ATPase in microsomal fractions and in preparations of purified Na,K-ATPase from duck salt glands. Incubation of melittin with these preparations also led to the progressive loss of Na,K-ATPase activity. At melittin/protein molar ratio of 5:1, we did not observe inhibition of Na,K-ATPase in the microsomal fraction but the process of enzyme aggregation occurred. At higher melittin/protein molar ratios (10:1 and 30:1), the inhibition of the enzyme and its aggregation proceeded simultaneously but the rates of these processes and maximal values achieved were different. At a melittin/protein ratio of 30:1, Na,K-ATPase inhibition may be described as a biexponential curve with the values for pseudo-first order rate constants being 2.7 and 0.15 min(-1). However, the aggregation may be presented by a monoexponential curve with a pseudo-first order rate constant of 0.15 min(-1). In purified preparations of Na,K-ATPase, the maximal aggregation (about 90%) was achieved at a melittin/protein molar ratio of 2:1, and a further increase in the melittin/protein ratio increased the rate of aggregation but did not affect the value of maximal aggregation. The results show that melittin induced both aggregation and inhibition of Na,K-ATPase but these two processes proceeded independently. (C) 2004 Elsevier B.V. All rights reserved.
- Добавил в систему: Рубцов Александр Михайлович