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PREPARATION OF MONOPEGYLATED HUMAN INTERFERON BETA-1A: OPTIMIZATION OF THE CONDITIONS FOR N-TERMINAL PEGYLATIONстатья
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: 23 января 2018 г.
- Авторы: Korzhavin D.V., Chernovskaya T.V., Efanov Y.G., Rudenko E.G., Ivanov R.A., Pshenichnikova A.B., Shvets V.I.
- Журнал: Applied Biochemistry and Microbiology
- Том: 51
- Номер: 7
- Год издания: 2015
- Издательство: Maik Nauka/Interperiodica Publishing
- Местоположение издательства: Russian Federation
- Первая страница: 774
- Последняя страница: 785
- DOI: 10.1134/S0003683815070030
- Аннотация: The recombinant human interferon (IFN) beta-1a was modified with polyethylene glycol (PEG). The reaction was performed with the use of activated linear butyraldehyde PEG derivative with a molecular weight of 30 kDa. As a result of the multifactorial experiment, the correlation between the reaction conditions and the yield of the monoPEGylated protein was demonstrated and the optimal PEGylation conditions were established. We developed a one-step chromatographic purification scheme that makes it possible to obtain monoPEG-IFN beta-1a conjugate a purity above 98%. Mass-spectrometric studies showed that the purified conjugate is the PEGylated IFN beta-1a, in which the N-terminal methionine is bound with a PEG molecule. The molecular weight of the conjugate is 54130 Da. The obtained PEG-IFN beta-1a has a specific antiviral activity; it can be considered as a promising candidate in the design of prolonged-release medicine for the treatment of multiple sclerosis.
- Добавил в систему: Черновская Татьяна Вениаминовна