Large-scale chromatography of recombinant proteins.
When recombinant proteins are expressed in bacterial cells and subsequently grown in fermentation tanks, there remains the problem of recovering the product in pure form. The empirical knowledge gained upon recovery of recombinant proteins indicates that a one-step purification process is very unlikely to succeed. However, combinations of modern techniques, such as immunoaffinity chromatography or immobilized-metal affinity chromatography, with classical techniques, such as ion-exchange chromatography, seem to be suitable for large-scale recovery of recombinant proteins.
Hochuli
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Central Research Units, F. Hoffmann-La Roche & Co., Ltd., Basle, Switzerland.
D002846:Chromatography, Affinity; D003300:Copper / Q000032:analysis; D004731:Endotoxins / Q000032:analysis; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D007136:Immunoglobulins / Q000032:analysis; D007163:Immunosorbent Techniques; D007370:Interferon Type I / Q000032:analysis; D009532:Nickel; D009571:Nitrilotriacetic Acid / Q000032:analysis; D011136:Polysorbates; D011994:Recombinant Proteins / Q000032:analysis*
D004731:Endotoxins; D007136:Immunoglobulins; D007370:Interferon Type I; D011136:Polysorbates; D011994:Recombinant Proteins; D003300:Copper; D009532:Nickel; D009571:Nitrilotriacetic Acid