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The influence of length and localization of polyhistidine tag in the molecule of organophosphorus hydrolase on the biosynthesis and behavior of fusion proteinстатья
- Авторы: Efremenko E.N., Lyagin I.V., Votchitseva Yu V., Gudkov D.A., Peregudov A.A., Aliev T.K., Varfolomeev S.D.
- Сборник: Biotechnology: State of the Art and Prospects for Development
- Глава в коллективной монографии
- Год издания: 2008
- Место издания: Nova Science Publishers Inc N.-Y
- Первая страница: 87
- Последняя страница: 101
- Аннотация: The influence of length and localization of polyhistidine sequence (polyHis-) genetically introduced into the molecule of organophosphorus hydrolase (OPH) on the biosynthesis and features of fusion protein was investigated. It was shown that independently on host strain of E. coli cells used for biosynthesis of target fusion proteins the 0.25 mM inductor concentration provided the highest yield of OPH analogues. The elongation of polyHis-tag introduced to OPH molecule resulted in 5-8 fold decrease in the yield of cell biomass independently on strain used for fusion protein biosynthesis. It was shown that both length and localization of polyHis-tag in the protein molecule were important for pH action profile of fusion enzymes based on OPH. The length of polyHistag appeared to be more important than its localization for temperature action profile of polyHis-OPH derivative and its efficiency of catalytic action in reactions with various organophosphorous compounds.
- Добавил в систему: Лягин Илья Владимирович