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[The role of the N-terminal fragment of troponin T in the interaction with troponin-tropomyosin complex components of the heart]статья
Информация о цитировании статьи получена из
Scopus
Дата последнего поиска статьи во внешних источниках: 28 мая 2015 г.
- Авторы: Verin A.D., Gusev N.B.
- Журнал: Biokhimii∎a (Moscow, Russia)
- Том: 53
- Номер: 8
- Год издания: 1988
- Издательство: IZDATELSTVO NAUKA
- Местоположение издательства: LENINGRADSKOE OTDELENIE MAKAROVA D4, STPETERSBURG, RUSSIA
- Первая страница: 1235
- Последняя страница: 1246
- Аннотация: Bovine heart troponin T was hydrolyzed at the single cysteine residue. This procedure resulted in two peptides--a short N-terminal peptide (40-50 amino acid residues) and a long C-terminal peptide (240 amino acid residues). The C-terminal peptide was purified to homogeneity by ion-exchange chromatography; its properties were compared to those of intact troponin T. Data from circular dichroism spectroscopy suggest that the short N-terminal peptide cleavage was unaccompanied by any conspicuous changes in the secondary structure of the large C-terminal peptide of troponin T. Unlike intact troponin T, its C-terminal peptide can interact with troponin C in the presence of Ca2+. Data from affinity chromatography demonstrated that troponin I and tropomyosin more strongly interacted with native troponin T than with its C-terminal peptide. It is concluded that the short N-terminal peptide (40-50 residues) plays an essential role in cardiac troponin T interaction with troponin and tropomyosin components.
- Добавил в систему: Гусев Николай Борисович