High-Speed Purification of Recombinant Interleukin-11 by IMAC with Rigid Biporous Beads


Rigid biporous beads were prepared and modified by iminodiacetic acid (IDA) for application in immobilized metal affinity chromatography of proteins. The retention behavior of four model proteins on the metal chelate columns loaded with copper (II) and nickel (II) ions were studied. The separation of the four proteins by the Ni-IDA column at 40 cm.min−1 was realized within 2 min. His6-interluekin-11 (His6-IL-11) was also purified by the Ni-IDA column at 40 cm.min−1. The collected His6-IL-11 fraction showed a purity of about 80%. The results indicate that the IMAC with the biporous medium is promising for high-speed protein purification.

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Correspondence to Yan Sun.

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Wu, L., Gan, Y. & Sun, Y. High-Speed Purification of Recombinant Interleukin-11 by IMAC with Rigid Biporous Beads. Chroma 63, 379 (2006). https://doi.org/10.1365/s10337-006-0761-6

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  • Immobilized metal affinity chromatography
  • Flow-through chromatography
  • Biporous stationary phase
  • Recombinant protein
  • Interleukin-11