Magnetic Affinity Separation of Recombinant Fusion Proteins

Yıl 2010, Cilt: 38 Sayı: 1, 1 - 7, 01.01.2010

Ivo Safarik Mirka Safarikova

Öz

Isolation and separation of proteins is an important procedure in all areas of biosciences and biotechnology. Currently recombinant fusion proteins are produced routinely; in order to simplify their isolation from complex samples, magnetic separation techniques can be efficiently used. This short review paper shows examples of the most important fusion affinity tags and commercially available magnetic affinity and ion exchange particles enabling efficient capture of recombinant fusion proteins. A list of realized isolation procedures documents the efficiency of magnetic separation techniques.

Anahtar Kelimeler

Recombinant fusion proteins, Affinity tags, Magnetic separation, Magnetic adsorbents

Kaynakça

• Jonasson, P., Liljeqvist, S., Nygren, P.A., Stahl, S., Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli, Biotechnol. Appl. Biochem. 35, 91, 2002.
• Safarik, I., Safarikova, M., Magnetic techniques for the isolation and purification of proteins and peptides, Biomagn. Res. Technol., 2, Article No. 7, 2004.
• Franzreb, M., Siemann-Herzberg, M., Hobley, T.J., Thomas, O.R.T., Protein purification using magnetic adsorbent particles, Appl. Microbiol. Biotechnol., 70, 505, 2006.
• Xie, H., Guo, X.M., Chen, H., Making the most of fusion tags technology in structural characterization of membrane proteins. Mol. Biotechnol., 42, 135, 2009.
• New England BioLabs, http://www.neb.com/nebecomm/ tech_reference/gene_expression_cellular_analysis/SNAP_ tag_technologies.asp. Lin, C.T., Moore, P.A., Auberry, D.L., Landorf, E.V., Peppler, T., Victry, K.D., Collart, F.R., Kery, V.: Automated purification of recombinant proteins: Combining high-throughput with high yield. Protein Expr. Purif., 47, 16, 2006.
• Huang, X.Y., Chao, D.Y., Gao, J.P., Zhu, M.Z., Shi, M., Lin, H.X., A previously unknown zinc finger protein, DST, regulates drought and salt tolerance in rice via stomatal aperture control, Genes Dev., 23, 1805, 2009.
• Belien, T., Van Campenhout, S., Van Acker, M., Volckaert, G., Cloning and characterization of two endoxylanases from the cereal phytopathogen Fusarium graminearum and their inhibition profile against endoxylanase inhibitors from wheat, Biochem. Biophys. Res. Commun., 327, 407, 2005.
• Belien, T., Hertveldt, K., Van den Brande, K., Robben, J., Van Campenhout, S., Volckaert, G., Functional display of family 11 endoxylanases on the surface of phage M13, J. Biotechnol., 115, 249, 2005.
• Lanzillotti, R., Coetzer, T.L., The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 protein. Malaria J., 5, Article No. 100, 2006.
• Meng, J., Walter, J.G., Kokpinar, O., Stahl, F., Scheper, T., Automated microscale His-tagged protein purification using Ni-NTA magnetic agarose beads. Chem. Eng. Technol., 31, , 2008.
• Redaelli, L., Zolezzi, F., Nardese, V., Bellanti, B., Wanke, V., Carettoni, D., A platform for high-throughput expression of recombinant human enzymes secreted by insect cells, J. Biotechnol., 120, 59, 2005.
• Lauterbach, S.B., Coetzer, T.L., The M18 aspartyl aminopeptidase of Plasmodium falciparum binds to human erythrocyte spectrin in vitro. Malaria J., 7, Article No. 161, Shanado, Y., Kometani, M., Uchiyama, H., Koizumi, S., Teno, N., Lysophospholipase I identified as a ghrelin deacylation enzyme in rat stomach. Biochem. Biophys. Res. Commun., 325, 1487, 2004.
• Florio, C., Moscariello, M., Ederle, S., Fasano, R., Lanzuolo, C., Pulitzer, J.F., A study of biochemical and functional interactions of Htl1p, a putative component of the Saccharomyces cerevisiae, Rsc chromatin-remodeling complex, Gene, 395, 72, 2007.
• Peipp, M., Simon, N., Loichinger, A., Baum, W., Mahr, K., Zunino, S.J., Fey, G.H., An improved procedure for the generation of recombinant single-chain Fv antibody fragments reacting with human CD13 on intact cells. J. Immunol. Methods, 251, 161, 2001.