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Rotational diffusion of bovine serum albumin denaturated by sodium dodecylsulfate, According to data from tryptophan fluorescenceстатья
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: 30 апреля 2014 г.
- Авторы: Vlasova I.M., Zhuravleva V.V., Saletskii A.M.
- Журнал: Russian Journal of Physical Chemistry A
- Том: 88
- Номер: 3
- Год издания: 2014
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 551
- Последняя страница: 556
- DOI: 10.1134/S003602441403025X
- Аннотация: The rotational diffusion of bovine serum albumin (BSA) molecules in solutions with different concentrations of the anionic detergent sodium dodecylsulfate (SDS) at different pH values is investigated, yielding information on the denaturation of BSA under the action of SDS. It is found from the increased degree of polarization in the tryptophan fluorescence of BSA and the registered parameters for the rotational diffusion of BSA molecules that the denaturation of BSA under the action of SDS at pH values less than the isoelectric point (pI) of BSA (4-9) is a two-stage process. It is shown that the first stage of BSA denaturation common for all pH values is the decondensation of BSA globules, while the second stage of BSA denaturation at pH greater than the pI of BSA is the unfolding of the protein's amino acid chain. It is concluded that the denaturation of BSA under the action of SDS proceeds more deeply at pH values greater than the pI of BSA.
- Добавил в систему: Салецкий Александр Михайлович