| 摘要 |
<p>Transforming growth factor β (TGF-β) is produced in relatively large quantities and at a relatively high purity by fermentation in a perfusion microcarrier reactor. Conditioned media from the reactor is first treated to provide the active form of TGF-β and subsequently purified by cation exchange chromatography followed by hydrophobic interaction chromatography. Optionally, nucleic acids complexed with the TGF-β may be removed while the protein is bound to the cation exchange resin. Purified TGF-β1 compositions have a specific activity above 107 U/ml.</p> |
