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Интеллектуальная Система Тематического Исследования НАукометрических данных |
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[Various properties of cardiac troponin C tryptic peptides]статья
Дата последнего поиска статьи во внешних источниках: 29 мая 2015 г.
- Авторы: Verin A.D., Baratova L.A., Gusev N.B.
- Журнал: Biochemistry (Moscow)
- Том: 53
- Номер: 7
- Год издания: 1988
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 1069
- Последняя страница: 1077
- Аннотация: Using chromatography and preparative polyacrylamide gel electrophoresis, tryptic peptides TP 1 (residues 47-83), TP 2 (residues 84-118) and TP 3 (residues 119-161) were isolated in a highly homogeneous state from cardiac troponin C. Peptides TP 1, TP 2 and TP 3 were found to contain isolated cation-binding sites II, III and IV of cardiac troponin C. The interaction of these peptides with troponins I and T was studied. It was found that only peptide TP 2 could interact with troponin I. Neither of the peptides isolated interacted with troponin T. The cation-binding properties and structural peculiarities of peptide TP 1 were investigated. It was shown that despite its small size (37 amino acid residues), peptide TP 1 retained its ability to bind Ca2+ which caused conformational changes in the peptide structure. This was accompanied by changes in the electrophoretic mobility and absorption of TP 1 on phenyl-Sepharose.
- Добавил в систему: Гусев Николай Борисович