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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 Research
Molecular Genetics, Microbiology and Virology ( IF 0.4 ) Pub Date : 2020-01-01 , DOI: 10.3103/s0891416820010036
A. V. Gromov , M. S. Poponova , A. S. Karyagina

Here, we give an overview of purification of the recombinant BMP-2 produced in Escherichia coli and 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.

中文翻译:

在大肠杆菌中产生的重组人骨生长因子 BMP-2。第 1 部分:从蛋白质纯化到功效研究的实验模型

在这里,我们概述了在大肠杆菌中产生的重组 BMP-2 的纯化及其作为不同成骨材料成分的骨组织再生的功效。描述了这种异源系统中的蛋白质生产及其随后的纯化和重折叠,从而产生了活性蛋白质。BMP-2 源自原核细胞在成骨诱导中的功效与真核细胞中产生的功效相似,已在多种载体和动物模型的许多研究中得到证实。在这次审查中,使用了数据库 PubMed Central(美国国立卫生研究院的国家医学图书馆,NIH/NLM)、PubMed(NLM 国家生物技术信息中心,NCBI)和电子图书馆(科学电子图书馆)。
更新日期:2020-01-01
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