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目的:利用大肠杆菌表达可溶性hCTRP1球状功能区蛋白并分析其生物活性。方法:重组质粒转化大肠杆菌BL21-codonplus(DE3)菌株、IPTG(异丙基-β-D-硫代半乳糖苷)诱导表达并纯化。结果:hCTRP1球状区蛋白实现在大肠杆菌中的高水平表达,利用镍亲合纯化和分子筛纯化到重组蛋白,重组蛋白在细胞和动物水平上都具有生物活性。结论:利用大肠杆菌表达系统高效制备了具有生物活性的hCTRP1球状功能区蛋白。
OBJECTIVE: To express soluble hCTRP1 globular domain protein in Escherichia coli and analyze its biological activity. Methods: The recombinant plasmid was transformed into Escherichia coli BL21-codonplus (DE3) strain and induced by IPTG (isopropyl-β-D-thiogalactopyranoside). Results: The hCTRP1 globular domain protein was highly expressed in E. coli. The recombinant protein was purified by nickel affinity purification and molecular sieve. The recombinant protein was bioactive at both cellular and animal level. Conclusion: The hCTRP1 globular functional domain protein with high biological activity was prepared efficiently by using E. coli expression system.