Expression and Purification of Recombinant Human Bone Morphogenetic Protein-7 (rhBMP-7) in Bacillus subtilis

고초균을 이용한 재조합 인간 골 형성 단백질-7의 발현과 정제

  • Kim, Chun-Kwang (Department of Material and Biochemical Engineering, Chonnam National University) ;
  • Oh, Sung-Duk (Research Center for Biophotonics, Chonnam National University) ;
  • Rhee, Jong-Il (School of Applied Chemical Engineering, Chonnam National University)
  • 김춘광 (전남대학교 물질.생물화학공학과) ;
  • 오성덕 (전남대학교 바이오광사업단) ;
  • 이종일 (전남대학교 응용화학공학부)
  • Received : 2009.09.04
  • Accepted : 2010.05.15
  • Published : 2010.06.30

Abstract

Bone morphogenetic protein-7 (BMP-7) is one of important growth factors for skeletal development and bone growth. In this work, BMP-7 was efficiently expressed in recombinant Bacillus subtilis. The mature BMP-7 protein indicated molecular weight of 15.4 kDa by Western blot assay and was secreted into culture medium with 0.35 ng/mL. The extracellular and intracellular rhBMP-7 proteins were purified by using a FPLC system with an ion exchange column and a gel filtration column. The extracellular and intracellular rhBMP-7 proteins had finally a 57.1% purity and a 36.2% purity, respectively. The purified rhBMP-7 proteins showed an intact biological activity which stimulated alkaline phophatase (ALP) activity in MC3T3-E1 cells.

Keywords

References

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