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Recombinant Human Bone Growth Factor BMP-2 Produced inEscherichia coli. Part 1: From Protein Purification to Experimental Models for Efficacy Research

期刊

出版社

ALLERTON PRESS INC
DOI: 10.3103/S0891416820010036

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BMP-2; Escherichia coli; protein isolation and purification; bone tissue regeneration; osteoplastic materials; review

资金

  1. Russian Scientific Foundation [16-15-00133]

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Here, we give an overview of purification of the recombinant BMP-2 produced inEscherichia 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.

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