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- W2368175958 abstract "AIM: To optimize the refolding of recombinant human bone morphogenetic protein-2 mature peptide(rhBMP-2m) in high protein concentration.METHODS: The engineered strain,which could express rhBMP-2m at a high level,was fermented in high density,and induced by temperature.The bacterial cells were collected and analyzed.The gained inclusion bodies were purified by ion-exchange chromatography.The purified rhBMP-2m was refolded by different dialysis methods,especially changing the pH,temperature,oxidize-reduced pair and ion concentration.After that,the refolding results were analyzed by non-reducing SDS-PAGE.The refolding rhBMP-2m passed through a 0.22 μm micropore filter membrane for degermation,and then the loss percentage was analyzed.RESULTS: The refolding rhBMP-2m was completely soluble,and more than 30% of rhBMP-2m dimmer were obtained corresponding to 800 mg rhBMP-2m dimmer per liter of culture broth,and the dimmer percent of refolding rhBMP-2m was remained after degerming by micropore filter membrane.At the same time,protein quantitative analysis showed that the loss of refolding rhBMP-2m was no more than 100 g/L.CONCLUSION: Changing pH during the refolding process can make the refolding production completely soluble,and the high pH is beneficial for refolding and low pH keeps the refolding rhBMP-2m soluble even if removing the deforming agent Urea from the high concentration of the refolding protein.The concentration of the protein,pH and the temperature affect the refolding significantly,while the concentration of ion and oxidize-reduced pair,and volume of dialysis refolding buffer have little effect." @default.
- W2368175958 created "2016-06-24" @default.
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- W2368175958 date "2008-01-01" @default.
- W2368175958 modified "2023-09-24" @default.
- W2368175958 title "Refolding of recombinant human bone morphogenetic protein-2 mature peptide in high concentration" @default.
- W2368175958 hasPublicationYear "2008" @default.
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