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ELPs标签纯化重组蛋白的研究进展

Research Progress in Purification of Recombinant Protein with Elastin-Like Polypeptides Tag
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摘要 分离纯化是重组蛋白生产的重要步骤,纯化标签的应用大大简化了重组蛋白的分离纯化过程,降低了生产成本。类弹性蛋白多肽(elastin-like polypeptides,ELPs)是近十几年发展起来的一种不依赖层析柱的快速、低成本生产重组蛋白的纯化标签。该标签是利用ELPs的可逆相变特性纯化重组蛋白,只需要离心即可进行大规模纯化重组蛋白。综述了ELPs标签相变条件的优化、ELPs标签与靶蛋白重组方式的优化、ELPs标签的切除及ELPs标签在纯化重组蛋白中的应用的研究进展。 Separation and purification are important steps in the production of recombinant protein.The application of purification tag has greatly simplified the separation and purification process of recombinant protein and reduced the production cost.Elastin-like polypeptides(ELPs)is a fast and low-cost purification tag independent of chromatography for the production of recombinant protein in the past 10 years.In the tag,the reversible phase transition property of ELPs is used to purify the recombinant protein,and thus only centrifugation is needed for the large-scale separation and purification of recombinant protein.We review the research progress in the optimization of phase transition conditions of ELPs tag,the optimization of the recombination mode of ELPs tag and target protein,the removal of ELPs tag,and the application of ELPs tag in the purification of recombinant protein.
作者 姜媛 丁宁 胡学军 JIANG Yuan;DING Ning;HU Xuejun(Medical College,Dalian University,Dalian 116000,China;Medical Research Center,Dalian University,Dalian 116622,China)
出处 《化学与生物工程》 CAS 2021年第3期14-19,共6页 Chemistry & Bioengineering
基金 国家自然科学基金项目(31470813,32070936),辽宁省科技厅项目(2019-ZD-0563)。
关键词 类弹性蛋白多肽标签 可逆相变温度 可逆相变循环技术 蛋白质纯化 ELPs tag inverse transition temperature(ITT) inverse transition cycle(ITC)technique protein purification
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  • 1Terpe K. Overview of tag protein fusions : from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Bioteehnol, 2003, 60 ( 5 ) : 523-533.
  • 2Urry DW. Free energy transduetion in polypeptides and proteins based on inverse temperature transitions. Prog Biophys Mol Biol, 1992, 57 ( 1 ) : 23-57.
  • 3Urry DW. Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers. J Phys Chem B, 1997, 101 ( 51 ) : 11007-11028.
  • 4Urry DW. Entropic elastic processes m protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics. J Protein Chem, 1988, 7 (1): 1-34.
  • 5Meyer DE, Chilkoti A. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol, 1999, 17 ( 11 ) : 1112-1115.
  • 6Scheller J, Henggeler D, Viviani A, et al. Purification of spider silk- elastin from transgenic plants and application for human chondrocyte proliferation. Transgenic Res, 2004, 13 ( 1 ) : 51-57.
  • 7Ge X, Yang DS, Trabhic-Carison K, et al. Self-cleavable stimulus responsive tags for protein purification without chromatography. J Am Chem Soc, 2005, 127 (32) : 11228-11229.
  • 8Banki MR, Feng L, Wood DW. Simple bioseparations using self- cleaving elastin-like polypeptide tags. Nat Methods, 2005, 2 ( 9 ) : 659-661.
  • 9Christensen T, Amiram M, Dagher S, et al. Fusion order controls expression level and activity of clastin-like polypeptide fusion proteins. Protein Sei, 2009, 18 ( 7 ) : 1377-1387.
  • 10Trabbie-Carison K, Liu L, Kim B, et al. Expression and purification of recombinant proteins from Escherichia eoli : Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion. ProteinSci, 2004, 13 ( 12 ) : 3274-3284.

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