Separation of antigens and antibodies by immunoaffinity chromatography

References

• Arutyunova EI, Arutyunov DY, Pleten’ AP, Nagradova NK, Muronetz VI. (2004). Antibodies specific to modified glyceraldehyde-3-phosphate dehydrogenase induce inactivation of the native enzyme and change its conformation. Biochim Biophys Acta, 1700, 35–41.
   Google Scholar
• Bibi E. (1989). Purification of TEM-1 beta-lactamase by immunoaffinity chromatography. Biochem J, 263, 309–311.
   Google Scholar
• Blank K, Lindner P, Diefenbach B, Plückthun A. (2002). Self-immobilizing recombinant antibody fragments for immunoaffinity chromatography: Generic, parallel, and scalable protein purification. Protein Expr Purif, 24, 313–322.
   PubMed Web of Science ®Google Scholar
• Bloom JW, Wong MF, Mitra G. (1989). Detection and reduction of protein A contamination in immobilized protein A purified monoclonal antibody preparations. J Immunol Methods, 117, 83–89.
   PubMed Web of Science ®Google Scholar
• Carter-Franklin JN, Victa C, McDonald P, Fahrner R. (2007). Fragments of protein A eluted during protein A affinity chromatography. J Chromatogr A, 1163, 105–111.
   PubMed Web of Science ®Google Scholar
• Cheng CA, John JA, Wu MS, Lee CY, Lin CH, Lin CH, Chang CY. (2006). Characterization of serum immunoglobulin M of grouper and cDNA cloning of its heavy chain. Vet Immunol Immunopathol, 109, 255–265.
   PubMed Web of Science ®Google Scholar
• Cossins AJ, Harrison S, Popplewell AG, Gore MG. (2007). Recombinant production of a VL single domain antibody in Escherichia coli and analysis of its interaction with peptostreptococcal protein L. Protein Expr Purif, 51, 253–259.
   Google Scholar
• Dainiak MB, Izumrudov VA, Muronetz VI, Galaev IY, Mattiasson B. (1998). Conjugates of monoclonal antibodies with polyelectrolyte complexes – an attempt to make an artificial chaperone. Biochim Biophys Acta, 1381, 279–285.
   Google Scholar
• D’Agostino B, Bellofiore P, De Martino T, Punzo C, Rivieccio V, Verdoliva A. (2008). Affinity purification of IgG monoclonal antibodies using the D-PAM synthetic ligand: Chromatographic comparison with protein A and thermodynamic investigation of the D-PAM/IgG interaction. J Immunol Methods, 333, 126–138.
   Google Scholar
• Dubrovskaya VV, Andryushkova AS, Kuznetsova IA, Toporkova LB, Buneva VN, Orlovskaya IA, Nevinsky GA. (2003). DNA-hydrolyzing antibodies from sera of autoimmune-prone MRL/MpJ-lpr mice. Biochemistry Mosc, 68, 1081–1088.
   Google Scholar
• Engström HA, Andersson PO, Ohlson S. (2005). Analysis of the specificity and thermodynamics of the interaction between low affinity antibodies and carbohydrate antigens using fluorescence spectroscopy. J Immunol Methods, 297, 203–211.
   Google Scholar
• Ghose S, Allen M, Hubbard B, Brooks C, Cramer SM. (2005). Antibody variable region interactions with protein A: implications for the development of generic purification processes. Biotechnol Bioeng, 92, 665–673.
   PubMed Web of Science ®Google Scholar
• Ghose S, Hubbard B, Cramer SM. (2006). Evaluation and comparison of alternatives to protein A chromatography Mimetic and hydrophobic charge induction chromatographic stationary phases. J Chromatogr A, 1122, 144–152.
   PubMed Web of Science ®Google Scholar
• Goldberg ME. (1991). Investigating protein conformation, dynamics and folding with monoclonal antibodies. Trends Biochem Sci, 16, 358–362.
   PubMedGoogle Scholar
• Grønborg M, Kristiansen TZ, Stensballe A, Andersen JS, Ohara O, Mann M, Jensen ON, Pandey A. (2002). A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, Frigg, as a protein kinase A substrate. Mol Cell Proteomics, 1, 517–527.
   PubMed Web of Science ®Google Scholar
• Guijarro JI, Jackson M, Chaffotte AF, Delepierre M, Mantsch HH, Goldberg ME. (1995). Protein folding intermediates with rapidly exchangeable amide protons contain authentic hydrogen-bonded secondary structures. Biochemistry, 34, 2998–3008.
   PubMed Web of Science ®Google Scholar
• Hahn R, Shimahara K, Steindl F, Jungbauer A. (2006). Comparison of protein A affinity sorbents III. Life time study. J Chromatogr A, 1102, 224–231.
   Google Scholar
• Hata T, Nakayama M. (2007). Rapid single-tube method for small-scale affinity purification of polyclonal antibodies using HaloTag Technology. J Biochem Biophys Methods, 70, 679–682.
   Google Scholar
• Hober S, Nord K, Linhult M. (2007). Protein A chromatography for antibody purification. J Chromatogr B Analyt Technol Biomed Life Sci, 848, 40–47.
   PubMed Web of Science ®Google Scholar
• Huang L, Fang X. (2008). Immunoaffinity fractionation of plasma proteins by chicken IgY antibodies. Methods Mol Biol, 425, 41–51.
   PubMedGoogle Scholar
• Jaoko WG, Lund M, Michael E, Simonsen PE. (2001). A simple and quick method for enhanced detection of specific IgE in serum from lymphatic filariasis patients. Acta Trop, 80, 51–57.
   Web of Science ®Google Scholar
• Josic D, Clifton JG. (2007). Use of monolithic supports in proteomics technology. J Chromatogr A, 1144, 2–13.
   Google Scholar
• Kabir S. (2002). Immunoglobulin purification by affinity chromatography using protein A mimetic ligands prepared by combinatorial chemical synthesis. Immunol Invest, 31, 263–278.
   PubMed Web of Science ®Google Scholar
• Kellogg DR, Alberts BM. (1992). Purification of a multiprotein complex containing centrosomal proteins from the Drosophila embryo by chromatography with low-affinity polyclonal antibodies. Mol Biol Cell, 3, 1–11.
   PubMedGoogle Scholar
• Kitao H, Takata M. (2006). Purification of TAP-tagged proteins by two-step pull down from DT40 cells. Subcell Biochem, 40, 409–413.
   Google Scholar
• Konovalova EV, Savvateeva EN, Dement’eva EI, Filippova MA, Turygin AIu, Osipova TV, Riabykh TP, Rubina AIu, Zasedatelev AS. (2007). [Development of a biochip for quantitative determination of two forms of prostate specific antigen using internal calibration curve]. Mol Biol (Mosk), 41, 734–738.
   Google Scholar
• Kuckelkorn U, Jacobasch G. (1990). Purification of pyruvate kinase from human erythrocytes by immunoaffinity chromatography. Biomed Biochim Acta, 49, S313–S316.
   Google Scholar
• Li R, Dowd V, Stewart DJ, Burton SJ, Lowe CR. (1998). Design, synthesis, and application of a protein A mimetic. Nat Biotechnol, 16, 190–195.
   PubMed Web of Science ®Google Scholar
• Liu FF, Dong XY, Wang T, Sun Y. (2007). Rational design of peptide ligand for affinity chromatography of tissue-type plasminogen activator by the combination of docking and molecular dynamics simulations. J Chromatogr A, 1175, 249–258.
   Google Scholar
• Lord CI, Riesselman MH, Gripentrog JM, Burritt JB, Jesaitis AJ, Taylor RM. (2008). Single-step immunoaffinity purification and functional reconstitution of human phagocyte flavocytochrome b. J Immunol Methods, 329, 201–207.
   PubMed Web of Science ®Google Scholar
• Martins S, Lourenço S, Karmali A, Serralheiro ML. (2007). Monoclonal antibodies recognize conformational epitopes on wild-type and recombinant mutant amidases from pseudomonas aeruginosa. Mol Biotechnol, 37, 136–145.
   Google Scholar
• Mikaelyan MV, Poghosyan GG, Gasparyan VK. (2008). Rapid purification of annexin V from human placenta by affinity chromatography. Prep Biochem Biotechnol, 38, 152–157.
   PubMed Web of Science ®Google Scholar
• Muronetz VI, Kazakov SV, Dainiak MB, Izumrudov VA, Galaev IY, Mattiasson B. (2000). Interaction of antibodies and antigens conjugated with synthetic polyanions: On the way of creating an artificial chaperone. Biochim Biophys Acta, 1475, 141–150.
   Google Scholar
• Muronetz VI, Korpela T. (2003). Isolation of antigens and antibodies by affinity chromatography. J Chromatogr B Analyt Technol Biomed Life Sci, 790, 53–66.
   PubMedGoogle Scholar
• Nedonchelle E, Pitiot O, Vijayalakshmi MA. (2000). A preliminary study for isolation of catalytic antibodies by histidine ligand affinity chromatography as an alternative to conventional protein A/G methods. Appl Biochem Biotechnol, 83, 287–294.; discussion 294
   PubMedGoogle Scholar
• Nikolaenko IV, Goncharenko VS, Shimko NN, Galkin AIu. (2007). [Isolation of surface antigen of hepatites B virus]. Ukr Biokhim Zh, 79, 114–122.
   Google Scholar
• Ning D, Junjian X, Xunzhang W, Wenyin C, Qing Z, Kuanyuan S, Guirong R, Xiangrong R, Qingxin L, Zhouyao Y. (2003). Expression, purification, and characterization of humanized anti-HBs Fab fragment. J Biochem, 134, 813–817.
   Google Scholar
• Omtvedt LA, Royle L, Husby G, Sletten K, Radcliffe CM, Harvey DJ, Dwek RA, Rudd PM. (2006). Glycan analysis of monoclonal antibodies secreted in deposition disorders indicates that subsets of plasma cells differentially process IgG glycans. Arthritis Rheum, 54, 3433–3440.
   Google Scholar
• O’Nuallain B, Allen A, Kennel SJ, Weiss DT, Solomon A, Wall JS. (2007). Localization of a conformational epitope common to non-native and fibrillar immunoglobulin light chains. Biochemistry, 46, 1240–1247.
   PubMed Web of Science ®Google Scholar
• Pagetta A, Tramentozzi E, Corbetti L, Frasson M, Brunati AM, Finotti P. (2007). Characterization of immune complexes of idiotypic catalytic and anti-idiotypic inhibitory antibodies in plasma of type 1 diabetic subjects. Mol Immunol, 44, 2870–2883.
   Google Scholar
• Palombo G, Verdoliva A, Fassina G. (1998). Affinity purification of immunoglobulin M using a novel synthetic ligand. J Chromatogr B Biomed Sci Appl, 715, 137–145.
   PubMed Web of Science ®Google Scholar
• Pandey A, Podtelejnikov AV, Blagoev B, Bustelo XR, Mann M, Lodish HF. (2000). Analysis of receptor signaling pathways by mass spectrometry: identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors. Proc Natl Acad Sci U S A, 97, 179–184.
   PubMed Web of Science ®Google Scholar
• Pappas D, Wang K. (2007). Cellular separations: A review of new challenges in analytical chemistry. Anal Chim Acta, 601, 26–35.
   Google Scholar
• Pavlovic M, Chen R, Kats AM, Cavallo MF, Saccocio S, Keating P, Hartmann JX. (2007). Highly specific novel method for isolation and purification of lupus anti-DNA antibody via oligo-(dT) magnetic beads. Ann N Y Acad Sci, 1108, 203–217.
   PubMed Web of Science ®Google Scholar
• Roque AC, Taipa MA, Lowe CR. (2005a). An artificial protein L for the purification of immunoglobulins and fab fragments by affinity chromatography. J Chromatogr A, 1064, 157–167.
   PubMed Web of Science ®Google Scholar
• Roque AC, Taipa MA, Lowe CR. (2005b). Synthesis and screening of a rationally designed combinatorial library of affinity ligands mimicking protein L from Peptostreptococcus magnus. J Mol Recognit, 18, 213–224.
   Google Scholar
• Roque AC, Silva CS, Taipa MA. (2007). Affinity-based methodologies and ligands for antibody purification: Advances and perspectives. J Chromatogr A, 1160, 44–55.
   PubMed Web of Science ®Google Scholar
• Steen H, Kuster B, Fernandez M, Pandey A, Mann M. (2002). Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. J Biol Chem, 277, 1031–1039.
   PubMed Web of Science ®Google Scholar
• Subramanian A. (2002). Immunoaffinity chromatography. Mol Biotechnol, 20, 41–47.
   PubMedGoogle Scholar
• Verdoliva A, Pannone F, Rossi M, Catello S, Manfredi V. (2002). Affinity purification of polyclonal antibodies using a new all-D synthetic peptide ligand: comparison with protein A and protein G. J Immunol Methods, 271, 77–88.
   PubMed Web of Science ®Google Scholar
• Taylor RM, Burritt JB, Foubert TR, Snodgrass MA, Stone KC, Baniulis D, Gripentrog JM, Lord C, Jesaitis AJ. (2003). Single-step immunoaffinity purification and characterization of dodecylmaltoside-solubilized human neutrophil flavocytochrome b. Biochim Biophys Acta, 1612, 65–75.
   Google Scholar
• Thompson NE, Burgess RR. (2001). Identification of polyol-responsive monoclonal antibodies for use in immunoaffinity chromatography. Curr Protoc Mol Biol, Chapter 11, Unit11.18.
   Google Scholar
• Upadhye V, Saha-Roy S, Shende N, Kumar S, Harinath BC. (2007). Isolation of Mycobacterium tuberculosis protein antigens ES-3 1, ES-43 and EST-6 of diagnostic interest from tubercle bacilli by affinity chromatography. Indian J Exp Biol, 45, 599–602.
   Google Scholar
• Verheesen P, ten Haaft MR, Lindner N, Verrips CT, de Haard JJ. (2003). Beneficial properties of single-domain antibody fragments for application in immunoaffinity purification and immuno-perfusion chromatography. Biochim Biophys Acta, 1624, 21–28.
   PubMedGoogle Scholar
• Warsinke A. (2008). Electrochemical biochips for protein analysis. Adv Biochem Eng Biotechnol, 109, 155–193.
   Google Scholar
• Xiao X, Yang X, Liu T, Chen Z, Chen L, Li H, Deng L. (2007). Preparing a highly specific inert immunomolecular-magnetic beads for rapid detection and separation of S. aureus and group G Streptococcus. Appl Microbiol Biotechnol, 75, 1209–1216.
   Google Scholar
• Yang L, Biswas ME, Chen P. (2003). Study of binding between protein A and immunoglobulin G using a surface tension probe. Biophys J, 84, 509–522.
   PubMed Web of Science ®Google Scholar
• Zhuang R, Zhang Y, Zhang R, Song C, Yang K, Yang A, Jin B. (2008). Purification of GFP fusion proteins with high purity and yield by monoclonal antibody-coupled affinity column chromatography. Protein Expr Purif, 59, 138–143.
   Google Scholar