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《海军军医大学学报》
>Non-fusion expression in Escherichia coli, purification, and characterization of a novel Ca^2＋- and phospho-lipid-binding protein annexin B1
Non-fusion expression in Escherichia coli, purification, and characterization of a novel Ca^2＋- and phospho-lipid-binding protein annexin B1
Annexin B1 is a novel member of the annexin family of Ca^2+- and phospholipid-binding proteins from Cysticercus cellulosae. To obtain high quality annexin B1 for biochemical and biophysical analyses, its cDNA was cloned into the prokaryotic expression vector pJLA503 and the translation initiation codon was immediately under the control of the inducible bacteriophage lambda promoters P(R) and P(L). Alter induction by shifting temperature, large amounts of non-fusion protein were produced in Escherichia coli in a soluble form. The recombinant protein was purified to homogeneity by means of two subsequent ion-exchange chromatographic steps. The final yield was about 25 mg/L bacterial culture.
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机译：The Evaluation for Anticancer Activity on Hep-2 and HepG-2 Cells of Ribosomal Protein L36 (RPL36) from the Escherichia coli BL21AU Hou, Yiling Ding, Xiang (starthlh@126.com) Hou, Wanru Wang, Ting Wang, Fang Li, Jian Zeng, Yichun
