Hochuli E
Central Research Units, F. Hoffmann-La Roche & Co., Ltd., Basle, Switzerland.
J Chromatogr. 1988 Jul 1;444:293-302. doi: 10.1016/s0021-9673(01)94032-4.
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.
当重组蛋白在细菌细胞中表达，随后在发酵罐中培养时，仍然存在以纯形式回收产物的问题。在重组蛋白回收过程中获得的经验知识表明，一步纯化过程极不可能成功。然而，现代技术如免疫亲和色谱或固定金属亲和色谱与经典技术如离子交换色谱的组合，似乎适用于重组蛋白的大规模回收。
