Bone induction by Escherichia coli -derived recombinant human bone morphogenetic protein-2 compared with Chinese hamster ovary cell-derived recombinant human bone morphogenetic protein-2

2000 ◽  
Vol 38 (6) ◽  
pp. 645-649 ◽  
Author(s):  
K. Bessho ◽  
Y. Konishi ◽  
S. Kaihara ◽  
K. Fujimura ◽  
Y. Okubo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bone Morphogenetic Protein ◽  
Chinese Hamster ◽  
Human Bone ◽  
Bone Morphogenetic Protein 2 ◽  
Ovary Cell ◽  
Bone Induction ◽  
Morphogenetic Protein ◽  
Human Bone Morphogenetic Protein ◽  
Recombinant Human Bone

scholarly journals Bone induction by recombinant human bone morphogenetic protein-2 with collagen as a carrier.

1998 ◽  
Vol 44 (12) ◽  
pp. 951-955
Author(s):  
Yasuzo KONISHI ◽  
Kazuhisa BESSHO ◽  
Kazuma FUJIMURA ◽  
Yasunori OKUBO ◽  
Kenji KUSUMOTO ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Human Bone ◽  
Bone Morphogenetic Protein 2 ◽  
Bone Induction ◽  
Morphogenetic Protein ◽  
Human Bone Morphogenetic Protein ◽  
Recombinant Human Bone

Soluble expression and purification of high-bioactivity recombinant human bone morphogenetic protein-2 by codon optimisation in Escherichia coli

2019 ◽  
Vol 32 (3) ◽  
pp. 153-157
Author(s):  
Wei Chen ◽  
Caiqian Zhang ◽  
Yeqing Wu ◽  
Xiuping Su
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Bone Morphogenetic Protein ◽  
Human Bone ◽  
Bone Morphogenetic Protein 2 ◽  
E Coli ◽  
Alp Activity ◽  
Morphogenetic Protein ◽  
Human Bone Morphogenetic Protein ◽  
Recombinant Human Bone

Abstract We developed a simple method of preparing recombinant human bone morphogenetic protein-2 (rhBMP-2) with high biological activity. This rhBMP-2 was overproduced in Escherichia coli as a fusion protein with thioredoxin 6xHis-tag at its amino terminus. The cDNA fragment of human bone morphogenetic protein-2 (hBMP-2) fused to the secretion signal of alkaline phosphatase (PhoA) was expressed under T7 promoter in E. coli. After DNA sequence confirmation, the recombinant vector pETpho-bmp2 was transformed into E. coli BL21 (DE3). rhBMP-2 was produced by the recombinant strain pETpho-bmp2/BL21 (DE3) in a soluble form with an yield of 6.2 mg/L culture. Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) results showed that the molecular weight of the product was approximately 28 kD. Moreover, rhBMP-2 was secreted as a dimer with a natural structure. rhBMP-2, purified by Ni Nitrilotriacetic acid Agarose (Ni-NTA) affinity chromatography, was used to examine osteosarcoma MG-63 cells and assay the alkaline phosphatase (ALP) activity. Results showed that rhBMP-2 induced MG-63 cell differentiation. When the final concentration was 500 ng/mL, the effect was more remarkable and ALP activity reached 525% compared with that of the control group.

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