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Liquid chromatography purification and study of uridilylpolynucleotide-(5’P-O) tyrosine phosphodiesteraseстатья
Информация о цитировании статьи получена из
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Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Yusupova R.A., Shatskaya G.S., Viryasov M.B., Drygin Yu F.
- Журнал: Chromatographia
- Том: 45
- Номер: 1
- Год издания: 1997
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 133
- Последняя страница: 137
- DOI: 10.1007/BF02505550
- Аннотация: LC has been used as a tool for studying uridilylpolynucleotide-(5′P→O)-phosphodiesterase—an enzyme which hydrolyses specifically the phosphodiester bond between picarnaviral RNA and viral protein VPg. According to various chromatographic data, the enzyme forms two types of complex with nucleic acids: weak ones which dissociate in 200 mM KCl, and others which are stable at concentrations up to 900 mM KCl. 2.5-3-fold (preparative) or 6-fold (normal scale) purification of the enzyme was obtained by size-exclusion chromatography (SEC). Cation-exchange separation (4-fold purification) was found to be more suitable as the second enzyme purification step than the earlier anionexchange method used. Three forms of enzyme activity were discovered by hydrophobic-interaction chromatography on the enzyme preparation obtained by SEC.
- Добавил в систему: Вирясов Михаил Борисович
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | chromatographia_1997.pdf | 418,1 КБ | 3 марта 2015 [viryasovmb] |