Covalent chromatography of influenza virus membrane M1 protein on activated thiopropyl Sepharose-6B

Fedorova, N.V.; Ksenofontov, A.L.; Viryasov, M.B.; Baratova, L.A.; Timofeeva, T.A.; Zhirnov, O.P.

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: 18 июля 2013 г.

Авторы: Fedorova N.V., Ksenofontov A.L., Viryasov M.B., Baratova L.A., Timofeeva T.A., Zhirnov O.P.
Журнал: Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Том: 706
Номер: 1
Год издания: 1998
Издательство: Elsevier BV
Местоположение издательства: Netherlands
Первая страница: 83
Последняя страница: 89
DOI: 10.1016/S0378-4347(97)00558-6
Аннотация: The M1 protein of influenza virus is a highly hydrophobic polypeptide that is resistant to enzyme cleavage during incubation in water solutions. We show here that the M1 protein that is immobilized on an insoluble activated support (thiopropyl Sepharose-6B) by means of a thiol–disulfide exchange reaction acquires sensitivity to trypsin. After tryptic digestion noncysteine-containing peptides of M1 were removed by washing the support, while cysteine-containing ones were detached from the support by reduction. As a result, 24 unique tryptic peptides of M1 protein were clearly separated by reversed-phase high-performance liquid chromatography. The described method opens a new way to the investigation of functional properties of distinct domains of viral thiol proteins.
Добавил в систему: Ксенофонтов Александр Леонидович

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Covalent chromatography of influenza virus membrane M1 protein on activated thiopropyl Sepharose-6Bстатья

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