Two variants of recombinant human bone morphogenetic protein-2 (rhBMP-2) with additional protein domains: Synthesis in an Escherichia coli heterologous expression system
| العنوان: | Two variants of recombinant human bone morphogenetic protein-2 (rhBMP-2) with additional protein domains: Synthesis in an Escherichia coli heterologous expression system |
|---|---|
| المؤلفون: | Anna S. Karyagina, Vladimir G. Lunin, O. V. Sergienko, A V Demidenko, T. M. Grunina, M. S. Poponova, I. S. Boksha, A. V. Gromov, A. M. Lyashchuk, Lyubov’ A. Soboleva, Z. M. Galushkina, M. S. Bartov, E. O. Osidak |
| المصدر: | Biochemistry (Moscow). 82:613-624 |
| بيانات النشر: | Pleiades Publishing Ltd, 2017. |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | 0301 basic medicine, Leucine zipper, 030102 biochemistry & molecular biology, Recombinant Fusion Proteins, Bone morphogenetic protein 8A, Protein domain, Bone Morphogenetic Protein 2, Gene Expression, Bone morphogenetic protein 10, General Medicine, Biology, Bovine pancreatic ribonuclease, Biochemistry, Bone morphogenetic protein 1, Cell Line, Mice, 03 medical and health sciences, Bone morphogenetic protein 6, Escherichia coli, biology.protein, Animals, Humans, Cattle, Heterologous expression |
| الوصف: | 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. |
| تدمد: | 1608-3040 0006-2979 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85f573a2c59d794ac2d46af1c2540106 https://doi.org/10.1134/s0006297917050091 |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi.dedup.....85f573a2c59d794ac2d46af1c2540106 |
| قاعدة البيانات: | OpenAIRE |
Find this article in full text from Springer Verlag. | تدمد: | 16083040 00062979 |
|---|