Paper Title:
Refolding and Purification of rhBMP-2 Expressed as Inclusion Bodies in E.COLI with Hydroxyapatite Chromatography
  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.

  Info
Periodical
Key Engineering Materials (Volumes 288-289)
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
S. Yao, L. L. Zhang, S. Y. Cheng, X. D. Zhang, "Refolding and Purification of rhBMP-2 Expressed as Inclusion Bodies in E.COLI with Hydroxyapatite Chromatography", Key Engineering Materials, Vols. 288-289, pp. 661-664, 2005
Online since
June 2005
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Price
$32.00
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