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- W2364203746 abstract "Objective: To obtain the high purity recombinant human osteogenic protein-1(rhOP-1) and assay the biologic activity of rhOP-1 expressed in Escherichia coli.Methods: The inclusion body was extracted through cracking the expression cells after fermentation of the Escherichia coli strain expressing human OP-1.The rhOP-1 was renatured by dialyzing and reducing the concentration of urea after purification by chromatography.NIH3T3 cells proliferation was assayed with improved MTT method and the activity of ALP was analyzed with PNPP method.At the same time,its activity was analyzed by implanting rhOP1 into thigh muscles of mouses in vivo.Results: The purity of rhOP-1 was about 98% after purification.The level of cells proliferation and ALP in the test group were significantly higher than that in the negative control group in vitro when the concentration of rhOP-1 varied from 0.06μg/ml to 6μg/ml.In vivo,the calcium content and the tendency of ossification in the group embeded with rhOP-1 into thigh muscles for two weeks were significantly elevated compared with the negative control.Conclusion: The rhOP-1 expressed in Escherichia coli has satisfactory biologic activity." @default.
- W2364203746 created "2016-06-24" @default.
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- W2364203746 date "2006-01-01" @default.
- W2364203746 modified "2023-09-23" @default.
- W2364203746 title "Purification and biological activity of the recombinatedhuman osteogenic protein-1" @default.
- W2364203746 hasPublicationYear "2006" @default.
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