Refolding and Purification of rhBMP-2 Expressed as Inclusion Bodies in E.COLI with Hydroxyapatite Chromatography |
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| Journal | Key Engineering Materials (Volumes 288 - 289) |
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| Volume | Advanced Biomaterials VI |
| Edited by | Xingdong Zhang, Junzo Tanaka, Yaoting Yu and Yasuhiko Tabata |
| Pages | 661-664 |
| DOI | 10.4028/www.scientific.net/KEM.288-289.661 |
| Citation | Shaohua Yao et al., 2005, Key Engineering Materials, 288-289, 661 |
| Online since | June, 2005 |
| Authors | Shaohua Yao, Ling Li Zhang, Steven Y. Cheng, Xing Dong Zhang |
| Keywords | Hydroxyapatite Chromatography, Inclusion Bodies, Purification, Refolding , rhBMP-2 |
| Abstract | The objective of this study was to develop an efficient method for the production of bioactive bone morphogenetic protein 2 (BMP-2). A recombinant plasmid encoding mature human BMP-2 was transferred and expressed at a high level in E.coli. Most of the aimed proteins existed in inclusion bodies. The non-active recombinant human BMP-2 (rhBMP-2) monomer in inclusion bodies was refolded and simultaneously purified using hydroxyapatite (HA) chromatography. After oxidization of the monomer, the rhBMP-2 dimmer showed biological activity by the induction of alkaline phosphate activity in C2C12 cells. The refolding yield was about 30% and the purity was about 90% just by one chromatography process. |
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