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Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragmentsстатья
Информация о цитировании статьи получена из
Scopus,
Web of Science
Дата последнего поиска статьи во внешних источниках: 4 марта 2022 г.
- Авторы: SEMISOTNOV Gennady V., VAS Maria, CHEMERIS Violetta V., KASHPAROVA Natalija J., KOTOVA Nina V., RAZGULYAEV Oleg I., SINEV Michael A.
- Журнал: European Journal of Biochemistry
- Том: 202
- Номер: 3
- Год издания: 1991
- Первая страница: 1083
- Последняя страница: 1089
- DOI: 10.1111/j.1432-1033.1991.tb16474.x
- Аннотация: The time course of refolding of both pig muscle and yeast 3-phosphoglycerate kinase (molecular masses about 47 kDa), as well as their proteolytic C-terminal fragments (30 and 33 kDa, respectively) has been investigated. Very similar refolding kinetics (with half-time between 80-120 s, at 20-degrees-C) were observed by fluorescence and ultraviolet absorbance spectroscopy, as well as by activity measurements, for the intact enzyme from both sources. This time course appears not to depend on the time the protein spends in the unfolded state, i.e. it is certainly not controlled by proline isomerization. Furthermore, after removal of a large N-terminal part (molecular mass of about 18 kDa for pig muscle enzyme or 13 kDa for yeast enzyme) of the molecule by proteolysis, refolding of the remaining C-terminal fragment of both proteins follows kinetics virtually indistinguishable from those of the intact protein molecule.
- Добавил в систему: Семисотнов Геннадий Васильевич