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Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actinстатья
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: Pivovarova A.V., Mikhailova V.V., Chernik I.S., Chebotareva N.A., Levitsky D.I., Gusev N.B.
- Журнал: Biochemical and Biophysical Research Communications
- Том: 331
- Номер: 4
- Год издания: 2005
- Издательство: Academic Press
- Местоположение издательства: United States
- Первая страница: 1548
- Последняя страница: 1553
- DOI: 10.1016/j.bbrc.2005.04.077
- Аннотация: Effect of recombinant chicken small heat shock protein with molecular mass 24 kDa (Hsp24) and recombinant human small heat shock protein with molecular mass 27 kDa (Hsp27) on the heat-induced denaturation and aggregation of skeletal F-actin was analyzed by means of differential scanning calorimetry and light scattering. All small heat shock proteins did not affect thermal unfolding of F-actin measured by differential scanning calorimetry, but effectively prevented aggregation of thermally denatured actin. Small heat shock protein formed stable complexes with denatured (but not with intact) F-actin. The size of these highly soluble complexes was smaller than the size of intact F-actin filaments. It is supposed that protective effect of small heat shock proteins on the cytoskeleton is at least partly due to prevention of aggregation of denatured actin. (c) 2005 Elsevier Inc. All rights reserved.
- Добавил в систему: Гусев Николай Борисович