Current affinity approaches for purification of recombinant proteins

References

• Akparov, V., Sokolenko, N., Timofeev, V., & Kuranova, I. (2015). Structure of the complex of carboxypeptidase B and N‐sulfamoyl‐L‐arginine. Acta Crystallographica Section F: Structural Biology Communications, 71(10), 1335–18.
   PubMedGoogle Scholar
• Andrews, B., Head, D., Dunthorne, P., & Asenjo, J. (1990). PEG activation and ligand binding for the affinity partitioning of proteins in aqueous two-phase systems. Biotechnology Techniques, 4(1), 49–54. doi:10.1007/BF00156610
   Google Scholar
• Antov, M., Anderson, L., Andersson, A., Tjerneld, F., & Stålbrand, H. (2006). Affinity partitioning of a Cellulomonas fimi β-mannanase with a mannan-binding module in galactomannan/starch aqueous two-phase system. Journal of Chromatography A, 1123(1), 53–59. doi:10.1016/j.chroma.2006.05.021
   PubMed Web of Science ®Google Scholar
• Arnau, J., Lauritzen, C., Petersen, G. E., & Pedersen, J. (2006). Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expression and Purification, 48(1), 1–13. doi:10.1016/j.pep.2005.12.002
   PubMed Web of Science ®Google Scholar
• Asliyuce, S., Mattiasson, B., & Mamo, G. (2016). Synthesis and use of protein G imprinted cryogel as affinity matrix to purify protein G from cell lyaste. Journal of Chromatography B, 1021, 204–212. doi:10.1016/j.jchromb.2015.12.060
   PubMed Web of Science ®Google Scholar
• Banki, M. R., Feng, L., & Wood, D. W. (2005). Simple bioseparations using self-cleaving elastin-like polypeptide tags. Nature Methods, 2(9), 659–662. doi:10.1038/nmeth738
   PubMed Web of Science ®Google Scholar
• Banki, M. R., Gerngross, T. U., & Wood, D. W. (2005). Novel and economical purification of recombinant proteins: Intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association. Protein Science: a Publication of the Protein Society, 14(6), 1387–1395. doi:10.1110/ps.041296305
   PubMed Web of Science ®Google Scholar
• Banki, M. R., Liang, F., & Wood, D. W. (2005). Simple bioseparations using self-cleaving elastin-like polypeptide tags. Nature Methods, 2(9), 659–662. doi:10.1038/nmeth738
   PubMed Web of Science ®Google Scholar
• Barbosa, H., Hine, A., Brocchini, S., Slater, N., & Marcos, J. (2008). Affinity partitioning of plasmid DNA with a zinc finger protein. Journal of Chromatography A, 1206(2), 105–112. doi:10.1016/j.chroma.2008.07.095
   PubMed Web of Science ®Google Scholar
• Beisson, F., Ferté, N., Voultoury, R., & Arondel, V. (2001). Large scale purification of an almond oleosin using an organic solvent procedure. Plant Physiology and Biochemistry, 39(7), 623–630. doi:10.1016/S0981-9428(01)01275-X
   Web of Science ®Google Scholar
• Brewer, S. J., & Sassenfeld, H. M. (1985). The purification of recombinant proteins using C-terminal polyarginine fusions. Trends in Biotechnology, 3(5), 119–122. doi:10.1016/0167-7799(85)90126-X
   Web of Science ®Google Scholar
• Cass, B., Pham, P. L., Kamen, A., & Durocher, Y. (2005). Purification of recombinant proteins from mammalian cell culture using a generic double-affinity chromatography scheme. Protein Expression and Purification, 40(1), 77–85. doi:10.1016/j.pep.2004.10.023
   PubMed Web of Science ®Google Scholar
• Cℏaga, G., Bochkariov, D. E., Jokhadze, G. G., Hopp, J., & Nelson, P. (1999). Natural poly-histidine affinity tag for purification of recombinant proteins on cobalt (II)-carboxymethylaspartate crosslinked agarose. Journal of Chromatography A, 864(2), 247–256. doi:10.1016/s0021-9673(99)01008-0
   PubMed Web of Science ®Google Scholar
• Chen, J. P., & Huffman, A. S. (1990). Polymer-protein conjugates: II. Affinity precipitation separation of human immunogammaglobulin by a poly (N-isopropylacrylamide)-protein A conjugate. Biomaterials, 11(9), 631–634. doi:10.1016/0142-9612(90)90020-q
   PubMed Web of Science ®Google Scholar
• Conley, A. J., Joensuu, J. J., Jevnikar, A. M., Menassa, R., & Brandle, J. E. (2009). Optimization of elastin‐like polypeptide fusions for expression and purification of recombinant proteins in plants. Biotechnology and Bioengineering, 103(3), 562–573. doi:10.1002/bit.22278
   PubMed Web of Science ®Google Scholar
• Conley, A. J., Joensuu, J. J., Richman, A., & Menassa, R. (2011). Protein body‐inducing fusions for high‐level production and purification of recombinant proteins in plants. Plant Biotechnology Journal, 9(4), 419–433. doi:10.1111/j.1467-7652.2011.00596.x
   PubMed Web of Science ®Google Scholar
• Conley, A. J., Mohib, K., Jevnikar, A. M., & Brandle, J. E. (2009). Plant recombinant erythropoietin attenuates inflammatory kidney cell injury. Plant Biotechnology Journal, 7(2), 183–199. doi:10.1111/j.1467-7652.2008.00389.x
   PubMed Web of Science ®Google Scholar
• Coolbaugh, M., Tang, M. S., & Wood, D. (2017). High-throughput purification of recombinant proteins using self-cleaving intein tags. Analytical Biochemistry, 516, 65–74. doi:10.1016/j.ab.2016.10.016
   PubMed Web of Science ®Google Scholar
• Dando, P. M., Fortunato, M., Strand, G. B., Smith, T. S., & Barrett, A. J. (2003). Pyroglutamyl-peptidase I: Cloning, sequencing, and characterisation of the recombinant human enzyme. Protein Expression and Purification, 28(1), 111–119.
   PubMed Web of Science ®Google Scholar
• Ding, Z., & Cao, X. (2013). Affinity precipitation of human serum albumin using a thermo-response polymer with an L-thyroxin ligand. BMC Biotechnology, 13(1), 109. doi:10.1186/1472-6750-13-109
   PubMedGoogle Scholar
• Fang, Y.-M., Lin, D.-Q., & Yao, S. J. (2018). Review on biomimetic affinity chromatography with short peptide ligands and its application to protein purification. Journal of Chromatography A, 1571, 1–15. doi:10.1016/j.chroma.2018.07.082
   PubMed Web of Science ®Google Scholar
• Floss, D. M., Sack, M., Arcalis, E., Stadlmann, J., Quendler, H., Rademacher, T., … & Conrad, U. (2009). Influence of elastin‐like peptide fusions on the quantity and quality of a tobacco‐derived human immunodeficiency virus‐neutralizing antibody. Plant Biotechnology Journal, 7(9), 899–913. doi:10.1111/j.1467-7652.2009.00452.x
   PubMed Web of Science ®Google Scholar
• Floss, D. M., Sack, M., Stadlmann, J., Rademacher, T., Scheller, J., Stöger, E., … & Conrad, U. (2008). Biochemical and functional characterization of anti‐HIV antibody–ELP fusion proteins from transgenic plants. Plant Biotechnology Journal, 6(4), 379–391. doi:10.1111/j.1467-7652.2008.00326.x
   PubMed Web of Science ®Google Scholar
• Frandsen, G. I., Mundy, J., & Tzen, J. T. (2001). Oil bodies and their associated proteins, oleosin and caleosin. Physiologia Plantarum, 112(3), 301–307.
   PubMed Web of Science ®Google Scholar
• Ge, X., Yang, D. S., Trabbic-Carlson, K., Kim, B., Chilkoti, A., & Filipe, C. D. (2005). Self-cleavable stimulus responsive tags for protein purification without chromatography. Journal of the American Chemical Society, 127(32), 11228–11229. doi:10.1021/ja0531125
   PubMed Web of Science ®Google Scholar
• Gingras, A. C., Aebersold, R., & Raught, B. (2005). Advances in protein complex analysis using mass spectrometry. The Journal of Physiology, 563(Pt 1), 11–21. doi:10.1113/jphysiol.2004.080440
   PubMed Web of Science ®Google Scholar
• Gong-Hong, W., De-Pei, L., & Liang, -C.-C. (2004). Charting gene regulatory networks: Strategies, challenges and perspectives. Biochemical Journal, 381(1), 1–12. doi:10.1042/BJ20040311
   PubMedGoogle Scholar
• Gräslund, S., Eklund, M., Falk, R., Uhlén, M., Nygren, P.-Å., & Ståhl, S. (2002). A novel affinity gene fusion system allowing protein A-based recovery of non-immunoglobulin gene products. Journal of Biotechnology, 99(1), 41–50.
   PubMed Web of Science ®Google Scholar
• Gu, H., Xu, K., Xu, C., & Xu, B. (2006). Biofunctional magnetic nanoparticles for protein separation and pathogen detection. Chemical Communications, (9), 941–949. doi:10.1039/b514130c
   PubMed Web of Science ®Google Scholar
• Guerrero, F., Ciragan, A., & Iwaï, H. (2015). Tandem SUMO fusion vectors for improving soluble protein expression and purification. Protein Expression and Purification, 116, 42–49. doi:10.1016/j.pep.2015.08.019
   PubMed Web of Science ®Google Scholar
• Hage, D. S., Anguizola, J. A., Li, R., Matsuda, R., Papastavros, E., Pfaunmiller, E. (2017). Affinity chromatography. Liquid chromatography (2nd ed., pp. 319–341). Amsterdam, the Netherlands: Elsevier.
   Google Scholar
• Healthcare, G. (2007). Recombinant protein purification handbook: Principles and methods. GE Healthcare Bio-Sciences AB, 14(6), 1–10.
   Google Scholar
• Hilbrig, F., & Freitag, R. (2003). Protein purification by affinity precipitation. Journal of Chromatography B, 790(1–2), 79–90. doi:10.1016/S1570-0232(03)00081-3
   PubMed Web of Science ®Google Scholar
• Jain, C. (2006). Overexpression and purification of tagged Escherichia coli proteins using a chromosomal knock-in strategy. Protein Expression and Purification, 46(2), 294–298. doi:10.1016/j.pep.2005.07.017
   PubMed Web of Science ®Google Scholar
• Joensuu, J. J., Conley, A. J., Lienemann, M., Brandle, J. E., Linder, M. B., & Menassa, R. (2010). Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana. Plant Physiology, 152(2), 622–633. doi:10.1104/pp.109.149021
   PubMed Web of Science ®Google Scholar
• Khoury, G. E., Khogeer, B., Chen, C., Ng, K. T., Jacob, S. I., & Lowe, C. R. (2015). Bespoke affinity ligands for the purification of therapeutic proteins. Pharmaceutical Bioprocessing, 3(2), 139–152. doi:10.4155/pbp.14.60
   Google Scholar
• Kimple, M. E., Brill, A. L., & Pasker, R. L. (2013). Overview of affinity tags for protein purification. Current Protocols in Protein Science, 73(1), 19–23.
   Google Scholar
• Korf, U., Kohl, T., van der Zandt, H., Zahn, R., Schleeger, S., Ueberle, B., .. & Wiemann, S. (2005). Large‐scale protein expression for proteome research. Proteomics, 5(14), 3571–3580. doi:10.1002/pmic.200401195
   PubMed Web of Science ®Google Scholar
• Kosobokova, E., Skrypnik, K., & Kosorukov, V. (2016). Overview of fusion tags for recombinant proteins. Biochemistry (Moscow), 81(3), 187–200. doi:10.1134/S0006297916030019
   PubMed Web of Science ®Google Scholar
• Lin, L.-J., Tai, S. S., Peng, -C.-C., & Tzen, J. T. (2002). Steroleosin, a sterol-binding dehydrogenase in seed oil bodies. Plant Physiology, 128(4), 1200–1211. doi:10.1104/pp.010928
   PubMed Web of Science ®Google Scholar
• Lin, Z., Zhao, Q., Xing, L., Zhou, B., & Wang, X. (2015). Aggregating tags for column‐free protein purification. Biotechnology Journal, 10(12), 1877–1886. doi:10.1002/biot.201500299
   PubMed Web of Science ®Google Scholar
• Linder, M. B., Qiao, M., Laumen, F., Selber, K., Hyytiä, T., Nakari-Setälä, T., & Penttilä, M. E. (2004). Efficient purification of recombinant proteins using hydrophobins as tags in surfactant-based two-phase systems. Biochemistry, 43(37), 11873–11882. doi:10.1021/bi0488202
   PubMed Web of Science ®Google Scholar
• Ling, Y.-Q., Nie, H.-L., Brandford-White, C., Williams, G. R., & Zhu, L.-M. (2012). Metal chelate affinity precipitation: Purification of BSA using poly (N-vinylcaprolactam-co-methacrylic acid) copolymers. Colloids and Surfaces B: Biointerfaces, 94, 281–287. doi:10.1016/j.colsurfb.2012.02.004
   PubMed Web of Science ®Google Scholar
• Lofdahl, S., Uhlen, M., Lindberg, M., & Sjoquist, J. (1992). Method of producing and isolating igg-binding protein a fusion peptides and a vector therefor. US5100788A.
   Google Scholar
• Loughran, S. T., & Walls, D. (2017). Tagging recombinant proteins to enhance solubility and aid purification. Protein chromatography (pp. 131–156). Berlin, Germany: Springer.
   Google Scholar
• Maestro, B., Velasco, I., Castillejo, I., Arévalo-Rodríguez, M., Cebolla, Á., & Sanz, J. M. (2008). Affinity partitioning of proteins tagged with choline-binding modules in aqueous two-phase systems. Journal of Chromatography A, 1208(1–2), 189–196. doi:10.1016/j.chroma.2008.08.106
   PubMed Web of Science ®Google Scholar
• Malakhov, M. P., Mattern, M. R., Malakhova, O. A., Drinker, M., Weeks, S. D., & Butt, T. R. (2004). SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins. Journal of Structural and Functional Genomics, 5(1–2), 75–86. doi:10.1023/B:JSFG.0000029237.70316.52
   PubMedGoogle Scholar
• Malhotra, A. (2009). Tagging for protein expression. Methods in Enzymology, 463, 239–258. doi:10.1016/S0076-6879(09)63016-0
   PubMed Web of Science ®Google Scholar
• Manjasetty, B. A., Turnbull, A. P., Panjikar, S., Büssow, K., & Chance, M. R. (2008). Automated technologies and novel techniques to accelerate protein crystallography for structural genomics. Proteomics, 8(4), 612–625. doi:10.1002/pmic.200700687
   PubMed Web of Science ®Google Scholar
• Marblestone, J. G., Edavettal, S. C., Lim, Y., Lim, P., Zuo, X., & Butt, T. R. (2006). Comparison of SUMO fusion technology with traditional gene fusion systems: Enhanced expression and solubility with SUMO. Protein Science : a Publication of the Protein Society, 15(1), 182–189. doi:10.1110/ps.051812706
   PubMed Web of Science ®Google Scholar
• Meyer, D. E., & Chilkoti, A. (1999). Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nature Biotechnology, 17(11), 1112–1115. doi:10.1038/15100
   PubMed Web of Science ®Google Scholar
• Meyer, D. E., & Chilkoti, A. (2004). Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides. Biomacromolecules, 5(3), 846–851. doi:10.1021/bm034215n
   PubMed Web of Science ®Google Scholar
• Meyer, D. E., Trabbic‐Carlson, K., & Chilkoti, A. (2001). Protein purification by fusion with an environmentally responsive elastin‐like polypeptide: Effect of polypeptide length on the purification of thioredoxin. Biotechnology Progress, 17(4), 720–728. doi:10.1021/bp010049o
   PubMed Web of Science ®Google Scholar
• Mohapatra, S., Pal, D., Ghosh, S. K., & Pramanik, P. (2007a). Design of superparamagnetic iron oxide nanoparticle for purification of recombinant proteins. Journal of Nanoscience and Nanotechnology, 7(9), 3193–3209. doi:10.1166/jnn.2007.869
   PubMed Web of Science ®Google Scholar
• Mohapatra, S., Pal, D., Ghosh, S. K., & Pramanik, P. J. (2007b). Design of superparamagnetic iron oxide nanoparticle for purification of recombinant proteins. Nanotechnology, 7(9), 3193–3199.
   Web of Science ®Google Scholar
• Nilsson, B., Holmgren, E., Josephson, S., Gatenbeck, S., Philipson, L., & Uhlen, M. (1985). Efficient secretion and purification of human insulin-like growth factor I with a gene fusion vector in Staphylococci. Nucleic Acids Research, 13(4), 1151–1162. doi:10.1093/nar/13.4.1151
   PubMed Web of Science ®Google Scholar
• Panavas, T., Sanders, C., & Butt, T. R. (2009). SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems. Methods in Molecular Biology (clifton, NJ), 497, 303–317.
   PubMedGoogle Scholar
• Peng, -C.-C., Chen, J. C., Shyu, D. J., Chen, M.-J., & Tzen, J. T. (2004). A system for purification of recombinant proteins in Escherichia coli via artificial oil bodies constituted with their oleosin-fused polypeptides. Journal of Biotechnology, 111(1), 51–57. doi:10.1016/j.jbiotec.2004.03.013
   PubMed Web of Science ®Google Scholar
• Peng, C. C., Lin, I., Lin, C. K., & Tzen, J. T. (2003). Size and stability of reconstituted sesame oil bodies. Biotechnology Progress, 19(5), 1623–1626. doi:10.1021/bp034129z
   PubMed Web of Science ®Google Scholar
• Perler, F. B. (2002). InBase: The intein database. Nucleic Acids Research, 30(1), 383–384. doi:10.1093/nar/30.1.383
   PubMed Web of Science ®Google Scholar
• Pina, A. S., Batalha, Í. L., & Roque, A. C. A. (2014). Affinity tags in protein purification and peptide enrichment: An overview. Protein downstream processing (pp. 147–168). Berlin, Germany: Springer.
   Google Scholar
• Porath, J., Carlsson, J., Olsson, I., & Belfrage, G. (1975). Metal chelate affinity chromatography, a new approach to protein fractionation. Nature, 258(5536), 598–610. doi:10.1038/258598a0
   PubMed Web of Science ®Google Scholar
• Porodko, A., Cirnski, A., Petrov, D., Raab, T., Paireder, M., Mayer, B., … & Schilling, O. (2018). The two cathepsin B-like proteases of Arabidopsis thaliana are closely related enzymes with discrete endopeptidase and carboxydipeptidase activities. Biological Chemistry 399. 1223–1235.
   PubMed Web of Science ®Google Scholar
• Prinz, B., Schultchen, J., Rydzewski, R., Holz, C., Boettner, M., Stahl, U., & Lang, C. (2004). Establishing a versatile fermentation and purification procedure for human proteins expressed in the yeasts Saccharomyces cerevisiae and Pichia pastoris for structural genomics. Journal of Structural and Functional Genomics, 5(1), 29–44. doi:10.1023/B:JSFG.0000029207.13959.90
   PubMedGoogle Scholar
• Rubio, V., Shen, Y., Saijo, Y., Liu, Y., Gusmaroli, G., Dinesh‐Kumar, S. P., & Deng, X. W. (2005). An alternative tandem affinity purification strategy applied to Arabidopsis protein complex isolation. The Plant Journal: For Cell and Molecular Biology, 41(5), 767–778. doi:10.1111/j.1365-313X.2004.02328.x
   PubMed Web of Science ®Google Scholar
• Ruiz-Ruiz, F., Benavides, J., Aguilar, O., & Rito-Palomares, M. (2012). Aqueous two-phase affinity partitioning systems: Current applications and trends. Journal of Chromatography A, 1244, 1–13. doi:10.1016/j.chroma.2012.04.077
   PubMed Web of Science ®Google Scholar
• Ruiz-Ruiz, F., Benavides, J., & Rito-Palomares, M. (2017). Affinity ATPS strategies for the selective fractionation of biomolecules. In Aqueous two-phase systems for bioprocess development for the recovery of biological products (pp. 97–121). Berlin, Germany: Springer.
   Google Scholar
• Sassenfeld, H. M., & Brewer, S. J. (1984). A polypeptide fusion designed for the purification of recombinant proteins. Nature Biotechnology, 2(1), 76–81. doi:10.1038/nbt0184-76
   Google Scholar
• Scheller, J., Leps, M., & Conrad, U. (2006). Forcing single‐chain variable fragment production in tobacco seeds by fusion to elastin‐like polypeptides. Plant Biotechnology Journal, 4(2), 243–249. doi:10.1111/j.1467-7652.2005.00176.x
   PubMed Web of Science ®Google Scholar
• Selber, K., Tjerneld, F., Collén, A., Hyytiä, T., Nakari-Setälä, T., Bailey, M., .. & Kula, M. R. (2004). Large-scale separation and production of engineered proteins, designed for facilitated recovery in detergent-based aqueous two-phase extraction systems. Process Biochemistry, 39(7), 889–896. doi:10.1016/S0032-9592(03)00198-5
   Web of Science ®Google Scholar
• Shah, N. H., & Muir, T. W. (2014). Inteins: Nature’s gift to protein chemists. Chemical Science, 5(2), 446–461. doi:10.1039/C3SC52951G
   PubMed Web of Science ®Google Scholar
• Shamji, M. F., Betre, H., Kraus, V. B., Chen, J., Chilkoti, A., Pichika, R., … & Setton, L. A. (2007). Development and characterization of a fusion protein between thermally responsive elastin‐like polypeptide and interleukin‐1 receptor antagonist: Sustained release of a local antiinflammatory therapeutic. Arthritis & Rheumatology, 56(11), 3650–3661. doi:10.1002/art.22952
   PubMedGoogle Scholar
• Shimazu, M., Mulchandani, A., & Chen, W. (2003). Thermally triggered purification and immobilization of elastin–OPH fusions. Biotechnology and Bioengineering, 81(1), 74–79. doi:10.1002/bit.10446
   PubMed Web of Science ®Google Scholar
• Sorgan, S., Miles, C., Chi-Chung, P., & Jason, T. (2002). Gene family of oleosin isoforms and their structural stabilization in sesame seed oil bodies. Bioscience, Biotechnology, and Biochemistry, 66(10), 2146–2153. doi:10.1271/bbb.66.2146
   PubMed Web of Science ®Google Scholar
• Southworth, M. W., Amaya, K., Evans, T. C., Xu, M.-Q., & Perler, F. B. (1999). Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein. Biotechniques, 27(1), 110–4, 6, 8–20. doi:10.2144/99271st04
   PubMed Web of Science ®Google Scholar
• Swartz, A. R. (2018). Functionalized nanoparticle crosslinking for enhanced affinity precipitation of monoclonal antibodies. Newark, US: University of Delaware.
   Google Scholar
• Teotia, S., Lata, R., & Gupta, M. (2004). Chitosan as a macroaffinity ligand: Purification of chitinases by affinity precipitation and aqueous two-phase extractions. Journal of Chromatography A, 1052(1–2), 85–91. doi:10.1016/j.chroma.2004.08.096
   PubMed Web of Science ®Google Scholar
• Terpe, K. (2003). Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems. Applied Microbiology and Biotechnology, 60(5), 523–533. doi:10.1007/s00253-002-1158-6
   PubMed Web of Science ®Google Scholar
• Trabbic‐Carlson, K., Liu, L., Kim, B., & Chilkoti, A. (2004). Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin‐like polypeptide fusion with an oligohistidine fusion. Protein Science: A Publication of the Protein Society, 13(12), 3274–3284. doi:10.1110/ps.04931604
   PubMed Web of Science ®Google Scholar
• Trabbic‐Carlson, K., Meyer, D., Liu, L., Piervincenzi, R., Nath, N., LaBean, T., & Chilkoti, A. (2004). Effect of protein fusion on the transition temperature of an environmentally responsive elastin‐like polypeptide: A role for surface hydrophobicity? Protein Engineering Design and Selection, 17(1), 57–66. doi:10.1093/protein/gzh006
   PubMed Web of Science ®Google Scholar
• Ullmann, A. (1984). One-step purification of hybrid proteins which have β-galactosidase activity. Gene, 29(1), 27–31. doi:10.1016/0378-1119(84)90162-8
   PubMed Web of Science ®Google Scholar
• Van Rooijen, G. J., & Moloney, M. M. (1995). Plant seed oil-bodies as carriers for foreign proteins. Biotechnology, 13(1), 72–77.
   PubMedGoogle Scholar
• Volkmann, G., & Mootz, H. D. (2013). Recent progress in intein research: From mechanism to directed evolution and applications. Cellular and Molecular Life Sciences, 70(7), 1185–1206. doi:10.1007/s00018-012-1120-4
   PubMed Web of Science ®Google Scholar
• Walls, D., & Loughran, S. T. (2011). Tagging recombinant proteins to enhance solubility and aid purification. In Dermot Walls and Sinéad T. Loughran (Eds.), Protein chromatography: Methods and protocols (pp. 151–175). Berlin, Germany: Springer.
   Google Scholar
• Wang, Z., Wu, H., Chen, J., Zhang, J., Yao, Y., & Chen, G.-Q. (2008). A novel self-cleaving phasin tag for purification of recombinant proteins based on hydrophobic polyhydroxyalkanoate nanoparticles. Lab on a Chip, 8(11), 1957–1962. doi:10.1039/b807762b
   PubMed Web of Science ®Google Scholar
• Waugh, D. S. (2005). Making the most of affinity tags. Trends in Biotechnology, 23(6), 316–320. doi:10.1016/j.tibtech.2005.03.012
   PubMed Web of Science ®Google Scholar
• Wingfield, P. T. (2015). Overview of the purification of recombinant proteins. Current Protocols in Protein Science, 80(1), 1–6. doi:10.1002/0471140864.ps0601s80
   PubMedGoogle Scholar
• Wood, D. W., & Camarero, J. A. (2014). Intein applications: From protein purification and labeling to metabolic control methods. The Journal of Biological Chemistry, 289(21), 14512–14529. doi:10.1074/jbc.R114.552653
   PubMed Web of Science ®Google Scholar
• Wood, D. W., Derbyshire, V., Wu, W., Chartrain, M., Belfort, M., & Belfort, G. (2000). Optimized single‐step affinity purification with a self‐cleaving intein applied to human acidic fibroblast growth factor. Biotechnology Progress, 16(6), 1055–1063. doi:10.1021/bp0000858
   PubMed Web of Science ®Google Scholar
• Wood, D. W., Wu, W., Belfort, G., Derbyshire, V., & Belfort, M. (1999). A genetic system yields self-cleaving inteins for bioseparations. Nature Biotechnology, 17(9), 889–892. doi:10.1038/12879
   PubMed Web of Science ®Google Scholar
• Xu, C., Xu, K., Gu, H., Zhong, X., Guo, Z., Zheng, R., & Xu, B. (2004). Nitrilotriacetic acid-modified magnetic nanoparticles as a general agent to bind histidine-tagged proteins. Journal of the American Chemical Society, 126(11), 3392–3403. doi:10.1021/ja031776d
   PubMed Web of Science ®Google Scholar
• Xu, M.-Q., & Evans, T. C. (2001). Intein-mediated ligation and cyclization of expressed proteins. Methods, 24(3), 257–277. doi:10.1006/meth.2001.1187
   PubMed Web of Science ®Google Scholar
• Yadav, D. K., Yadav, N., Yadav, S., Haque, S., & Tuteja, N. (2016). An insight into fusion technology aiding efficient recombinant protein production for functional proteomics. Archives of Biochemistry and Biophysics, 612, 57–77. doi:10.1016/j.abb.2016.10.012
   PubMed Web of Science ®Google Scholar
• Yang, X., Pistolozzi, M., & Lin, Z. (2018). New trends in aggregating tags for therapeutic protein purification. Biotechnology Letters, 40, 745–753. doi:10.1007/s10529-018-2543-2
   PubMed Web of Science ®Google Scholar
• Young, C. L., Britton, Z. T., & Robinson, A. S. (2012). Recombinant protein expression and purification: A comprehensive review of affinity tags and microbial applications. Biotechnology Journal, 7(5), 620–634. doi:10.1002/biot.201100155
   PubMed Web of Science ®Google Scholar
• Zhou, L., Wan, J., & Cao, X. (2010). Synthesis of thermo-sensitive copolymer with affinity butyl ligand and its application in lipase purification. Journal of Chromatography B, 878(15–16), 1025–1030. doi:10.1016/j.jchromb.2010.03.001
   PubMed Web of Science ®Google Scholar