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Isolation of rabbit liver heat shock protein with molecular weight 90 kD (Hsp90) and its interaction with troponin components and calponinстатья
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: 7 октября 2013 г.
- Авторы: Ma Y.S., Bogatcheva N.V., Gusev N.B.
- Журнал: Biochemistry (Moscow)
- Том: 63
- Номер: 11
- Год издания: 1998
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 1282
- Последняя страница: 1289
- Аннотация: Using a modified method consisting of chromatography on phenyl-Sepharose, Q-Sepharose, and hydroxyapatite, we isolated a highly purified heat shock protein with molecular weight 90 kD (Hsp90) from rabbit liver. The isolated protein was recognized on immunoblot by commercially available monoclonal anti-Hsp90 antibodies. The chromatographic properties, interaction with actin and calmodulin, phosphorylation in the presence of Mg-ATP, and one-dimensional peptide maps of rabbit liver Hsp90 are similar to the corresponding properties of Hsp90 isolated from other sources. In the presence of soluble carbodiimide and N-hydroxysuccinimide, rabbit liver Hsp90 can be cross-linked with calmodulin, troponin C, troponin I, and calponin. The data obtained indicate that Hsp90 may participate in the assembly of regulatory proteins of the actin filament.
- Добавил в систему: Гусев Николай Борисович