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Two variants of recombinant human bone morphogenetic protein_2 (rhBMP-2) with additional protein domains: synthesis in an Escherichia coli heterologous expression systemстатья
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: 28 ноября 2017 г.
- Авторы: Karyagina A.S., Boksha I.S., Grunina T.M., Demidenko A.V., Poponova M.S., Sergienko O.V., Lyashchuk A.M., Galushkina Z.M., Soboleva L.A., Osidak E.O., Bartov M.S., Gromov A.V., Lunin V.G.
- Журнал: Biochemistry (Moscow)
- Том: 82
- Номер: 5
- Год издания: 2017
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 613
- Последняя страница: 624
- DOI: 10.1134/S0006297917050091
- Аннотация: Two variants of recombinant human bone morphogenetic protein-2 (rhBMP-2) with additional N-terminal protein domains were obtained by expression in E. coli. The N-terminal domains were s-tag (15-a.a. oligopeptide from bovine pancreatic ribonuclease A) and lz (leucine zipper dimerization domain from yeast transcription factor GCN4). The s-tag-BMP-2 and lz-BMP-2 were purified by a procedure that excluded a long refolding stage. The resulting dimeric proteins displayed higher solubility compared to rhBMP-2 without additional protein domains. Biological activity of both proteins was demonstrated in vitro by induction of alkaline phosphatase in C2C12 cells, and the activity of s-tag-BMP-2 in vivo was shown in various experimental animal models.
- Добавил в систему: Карягина-Жулина Анна Станиславовна