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Separation and Purification of Annexin B1, a Novel Ca2+-Dependent Phospholipid Binding Protein, Expressed in Escherichia coli by Ion-Exchange Chromatography

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Summary

Annexin B1 has been cloned in Escherichia coli (E. coli) K802 in previous works. After temperature shift induction the protein was expressed as soluble form. Then a separation method for annexin B1 from E. coli cells by ion-exchange chromatography has been developed and validated. The method exhibited a good reproducibility and is easy to operate. It has shown that annexin B1 isolated by chromatography had high anticoagulant activity.

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Authors and Affiliations

  1. Department of Medical Genetics, The Second Military Medical University, Xiang Yin Road 800, Shanghai, 200433, P.R. China

    Yi Zhang, Yingjun Guo, Yuanjian Gao, Shu Zhang, Hongli Yan & Shuhan Sun

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  1. Yi Zhang
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  2. Yingjun Guo
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  3. Yuanjian Gao
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  4. Shu Zhang
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  5. Hongli Yan
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  6. Shuhan Sun
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Correspondence to Shuhan Sun.

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Zhang, Y., Guo, Y., Gao, Y. et al. Separation and Purification of Annexin B1, a Novel Ca2+-Dependent Phospholipid Binding Protein, Expressed in Escherichia coli by Ion-Exchange Chromatography. Chromatographia 58, 713–716 (2003). https://doi.org/10.1365/s10337-003-0107-6

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  • DOI: https://doi.org/10.1365/s10337-003-0107-6

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