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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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Ion exchange chromatography is widely used for protein purification due to several advantages including high speed and low cost. However, this method is not useful for purification of human rhinovirus 3C protease (HRV3C) and tobacco etch virus protease (TEVp) since they do not bind to both cation and anion exchange resins at physiological salt concentrations. Here we report a time- and cost-effective method for the purification of HRV3C and TEVp which ensures high purity and yield. The method entails fusion of 7Lys-tagged maltose-binding protein and 6His-tag to the N- and C-termini of two proteases, respectively, and leads to purification of highly pure protein using Ni-affinity and cation exchange chromatographies in less than 8 hours.
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참고문헌 (8)
참고문헌 신청
Bychkova, V. E. / 2014 / How membrane surface affects protein structure / Biochemistry (Mosc) 79:1483~1514
Cabrita, L. D. / 2007 / Enhancing the stability and solubility of TEV protease using in silico design / Protein Sci 16:2360~2367
Cesaratto, F. / 2015 / Engineered tobacco etch virus(TEV)protease active in the secretory pathway of mammalian cells / J Biotechnol 212:159~166
Champion, K. M. / 2001 / Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes / Proteomics 1:1133~1148
Kapust, R. B. / 2001 / Tobacco etch virus protease : mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency / Protein Eng 14:993~1000
Cabrita, L. D. / 2007 / Enhancing the stability and solubility of TEV protease using in silico design / Protein Sci 16:2360~2367
Cesaratto, F. / 2015 / Engineered tobacco etch virus(TEV)protease active in the secretory pathway of mammalian cells / J Biotechnol 212:159~166
Champion, K. M. / 2001 / Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes / Proteomics 1:1133~1148
Kapust, R. B. / 2001 / Tobacco etch virus protease : mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency / Protein Eng 14:993~1000
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