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Recombinant human bone growth factor BMP-2 produced in Escherichia coli. Part 1: from protein purification to experimental models for efficacy researchстатья
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: 17 июля 2020 г.
- Авторы: Gromov A.V., Poponova M.S., Karyagina A.S.
- Журнал: Molecular Genetics, Microbiology and Virology
- Том: 35
- Номер: 1
- Год издания: 2020
- Издательство: Allerton Press Inc.
- Местоположение издательства: United States
- Первая страница: 22
- Последняя страница: 31
- DOI: 10.3103/S0891416820010036
- Аннотация: Here, we give an overview of purification of the recombinant BMP-2 produced in Escherichia coliand its efficacy in bone tissue regeneration as a constituent of different osteoplastic materials. Protein production in this heterologous system and its subsequent purification and refolding resulting in the active protein are described. The efficacy of BMP-2 originated from prokaryotic cells in osteogenesis induction, which is similar to the efficacy of that produced in eukaryotic cells, has been demonstrated in many studies with the variety of carriers and animal models. In this review, the databases PubMed Central (United States National Institutes of Health’s National Library of Medicine, NIH/NLM), PubMed (NLM National Center for Biotechnology Information, NCBI), and e-library (Scientific Electronic Library) were used.
- Добавил в систему: Карягина-Жулина Анна Станиславовна