참고문헌
- Acchione, M., Kwon, H., Jochheim, C.M., and Atkins, W.M. 2012. Impact of linker and conjugation chemistry on antigen binding, fc receptor binding and thermal stability of model antibody-drug conjugates. MAbs. 4, 362-372. https://doi.org/10.4161/mabs.19449
- Carrier, A., Ducancel, F., Settiawan, N.B., Cattolico, L., Maillere, B., Leonetti, M., Drevet, P., Menez, A., and Boulain, J.C. 1995. Recombinant antibody-alkaline phosphatase conjugates for diagnosis of human iggs: Application to anti-hbsag detection. J. Immunol. Methods 181, 177-186. https://doi.org/10.1016/0022-1759(94)00344-V
- Coleman, J.E. 1992. Structure and mechanism of alkaline phosphatase. Ann. Rev. Biophy. Biomol. Struct. 21, 441-483. https://doi.org/10.1146/annurev.bb.21.060192.002301
- Ducancel, F., Gillet, D., Carrier, A., Lajeunesse, E., Menez, A., and Boulain, J.C. 1993. Recombinant colorimetric antibodies: construction and characterization of a bifunctional f (ab) 2/alkaline phosphatase conjugate produced in Escherichia coli. Biotechnology 11, 601-605. https://doi.org/10.1038/nbt0593-601
- Duenas, M., Vazquez, J., Ayala, M., Soderlind, E., Ohlin, M., Perez, L., Borrebaeck, C., and Gavilondo, J. 1994. Intra-and extracellular expression of an scFv antibody fragment in E. coli: effect of bacterial strains and pathway engineering using GroES/L chaperonins. BioTechniques 16, 476-477, 480-473.
- Harlow, E. and Lane, D. 1988. Antibodies: A lab manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA.
- Hu, Z.Q., Li, H.P., Zhang, J.B., Huang, T., Liu, J.L., Xue, S., Wu, A.B., and Liao, Y.C. 2013. A phage-displayed chicken single-chain antibody fused to alkaline phosphatase detects Fusarium pathogens and their presence in cereal grains. Anal. Chim. Acta. 764, 84-92. https://doi.org/10.1016/j.aca.2012.12.022
- Kim, J.K., Tsen, M.F., Ghetie, V., and Ward, E.S. 1994. Identifying amino acid residues that influence plasma clearance of murine IgG1 fragments by site-directed mutagenesis. Eur. J. Immunol. 24, 542-548. https://doi.org/10.1002/eji.1830240308
- Le Gall, F., Reusch, U., Little, M., and Kipriyanov, S.M. 2004. Effect of linker sequences between the antibody variable domains on the formation, stability and biological activity of a bispecific tandem diabody. Protein Eng. Des. Sel. 17, 357-366. https://doi.org/10.1093/protein/gzh039
- Lee, S.H., Park, D.W., Sung, E.S., Park, H.R., Kim, J.K., and Kim, Y.S. 2010. Humanization of an agonistic anti-death receptor 4 single chain variable fragment antibody and avidity-mediated enhancement of its cell death-inducing activity. Mol. Immunol. 47, 816-824. https://doi.org/10.1016/j.molimm.2009.09.041
- Lei, S.P., Lin, H., Wang, S.S., Callaway, J., and Wilcox, G. 1987. Characterization of the Erwinia carotovora pelB gene and its product pectate lyase. J. Bacteriol. 169, 4379-4383. https://doi.org/10.1128/jb.169.9.4379-4383.1987
- Liu, X., Wang, H., Liang, Y., Yang, J., Zhang, H., Lei, H., Shen, Y., and Sun, Y. 2010. Production and characterization of a single-chain Fv antibody-alkaline phosphatase fusion protein specific for clenbuterol. Mol. Biotechnol. 45, 56-64. https://doi.org/10.1007/s12033-010-9240-2
- Mandecki, W., Shallcross, M.A., Sowadski, J., and Tomazic-Allen, S. 1991. Mutagenesis of conserved residues within the active site of Escherichia coli alkaline phosphatase yields enzymes with increased kcat. Protein Eng. 4, 801-804. https://doi.org/10.1093/protein/4.7.801
- Muller, B.H., Chevrier, D., Boulain, J.C., and Guesdon, J.L. 1999. Recombinant single-chain Fv antibody fragment-alkaline phosphatase conjugate for one-step immunodetection in molecular hybridization. J. Immunol. Methods 227, 177-185. https://doi.org/10.1016/S0022-1759(99)00071-X
- Park, K.J., Park, D.W., Kim, C.H., Han, B.K., Park, T.S., Han, J.Y., Lillehoj, H.S., and Kim, J.K. 2005. Development and characterization of a recombinant chicken single-chain Fv antibody detecting Eimeria acervulina sporozoite antigen. Biotechnol. Lett. 27, 289-295. https://doi.org/10.1007/s10529-005-0682-8
- Sadeghi, H.M.M., Rabbani, M., and Fazeli, S. 2008. Optimization of alkaline phosphatase gene expression in E. coli. Res. Pharmaceut. Sci. 3, 35-39.
- Solar, I. and Gershoni, J.M. 1995. Linker modification introduces useful molecular instability in a single chain antibody. Protein Eng. 8, 717-723. https://doi.org/10.1093/protein/8.7.717
- Suzuki, C., Ueda, H., Suzuki, E., and Nagamune, T. 1997. Construction, bacterial expression, and characterization of hapten-specific single-chain fv and alkaline phosphatase fusion protein. J. Biochem. 122, 322-329. https://doi.org/10.1093/oxfordjournals.jbchem.a021756
- Trinh, R., Gurbaxani, B., Morrison, S.L., and Seyfzadeh, M. 2004. Optimization of codon pair use within the (ggggs)3 linker sequence results in enhanced protein expression. Mol. Immunol. 40, 717-722. https://doi.org/10.1016/j.molimm.2003.08.006
- Volkel, T., Korn, T., Bach, M., Muller, R., and Kontermann, R.E. 2001. Optimized linker sequences for the expression of monomeric and dimeric bispecific single-chain diabodies. Protein Eng. 14, 815-823. https://doi.org/10.1093/protein/14.10.815
- Wang, C.L., Huang, M., Wesson, C.A., Birdsell, D.C., and Trumble, W.R. 1994. A single Fc binding domain-alkaline phosphatase gene fusion expresses a protein with both IgG binding ability and alkaline phosphatase enzymatic activity. Protein Eng. 7, 715-722. https://doi.org/10.1093/protein/7.5.715
- Wang, S., Zheng, C., Liu, Y., Zheng, H., and Wang, Z. 2008. Construction of multiform scFv antibodies using linker peptide. J. Genet. Genomics 35, 313-316. https://doi.org/10.1016/S1673-8527(08)60045-4
- Wels, W., Harwerth, I.M., Zwickl, M., Hardman, N., Groner, B., and Hynes, N.E. 1992. Construction, bacterial expression and characterization of a bifunctional single-chain antibody-phosphatase fusion protein targeted to the human erbb-2 receptor. Biotechnology 10, 1128-1132. https://doi.org/10.1038/nbt1092-1128
- Whitlow, M., Bell, B.A., Feng, S.L., Filpula, D., Hardman, K.D., Hubert, S.L., Rollence, M.L., Wood, J.F., Schott, M.E., and Milenic, D.E. 1993. An improved linker for single-chain Fv with reduced aggregation and enhanced proteolytic stability. Protein Eng. 6, 989-995. https://doi.org/10.1093/protein/6.8.989
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