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Volumn 2, Issue , 2004, Pages

Magnetic techniques for the isolation and purification of proteins and peptides

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EID: 33751401429     PISSN: 1477044X     EISSN: 1477044X     Source Type: Journal    
DOI: 10.1186/1477-044X-2-7     Document Type: Review
Times cited : (460)

References (163)
  • 2
    • 0036000009 scopus 로고    scopus 로고
    • Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes
    • Hofmann I, Schnolzer M, Kaufmann I, Franke WW: Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes. Mol Biol Cell 2002, 13:1665-1676.
    • (2002) Mol Biol Cell , vol.13 , pp. 1665-1676
    • Hofmann, I.1    Schnolzer, M.2    Kaufmann, I.3    Franke, W.W.4
  • 3
    • 0032004884 scopus 로고    scopus 로고
    • Affinity chromatographic purification of antibodies to a biotinylated fusion protein expressed in Escherichia coli
    • Alche JD, Dickinson K: Affinity chromatographic purification of antibodies to a biotinylated fusion protein expressed in Escherichia coli. Protein Expr Purif 1998, 12:138-143.
    • (1998) Protein Expr Purif , vol.12 , pp. 138-143
    • Alche, J.D.1    Dickinson, K.2
  • 4
    • 0035070410 scopus 로고    scopus 로고
    • Purification of alpha-amylases using magnetic alginate beads
    • Teotia S, Gupta MN: Purification of alpha-amylases using magnetic alginate beads. Appl Biochem Biotechnol 2001, 90:211-220.
    • (2001) Appl Biochem Biotechnol , vol.90 , pp. 211-220
    • Teotia, S.1    Gupta, M.N.2
  • 5
  • 6
    • 69249216506 scopus 로고    scopus 로고
    • To bead or not to bead: Applications of magnetic bead technology
    • Sinclair B: To bead or not to bead: Applications of magnetic bead technology. Scientist 1998, 12:17.
    • (1998) Scientist , vol.12 , pp. 17
    • Sinclair, B.1
  • 8
    • 0024845760 scopus 로고
    • Antibodies immobilized on inorganic supports
    • Weetall HH, Lee MJ: Antibodies immobilized on inorganic supports. Appl Biochem Biotechnol 1989, 22:311-330.
    • (1989) Appl Biochem Biotechnol , vol.22 , pp. 311-330
    • Weetall, H.H.1    Lee, M.J.2
  • 9
    • 0027428893 scopus 로고
    • Batch isolation of hen egg white lysozyme with magnetic chitin
    • Safarik I, Safarikova M: Batch isolation of hen egg white lysozyme with magnetic chitin. J Biochem Biophys Methods 1993, 27:327-330.
    • (1993) J Biochem Biophys Methods , vol.27 , pp. 327-330
    • Safarik, I.1    Safarikova, M.2
  • 10
    • 0142169012 scopus 로고    scopus 로고
    • Magnetic alginate microparticles for purification of α-amylases
    • Safarikova M, Roy I, Gupta MN, Safarik I: Magnetic alginate microparticles for purification of α-amylases. J Biotechnol 2003, 105:255-260.
    • (2003) J Biotechnol , vol.105 , pp. 255-260
    • Safarikova, M.1    Roy, I.2    Gupta, M.N.3    Safarik, I.4
  • 11
    • 0033870977 scopus 로고    scopus 로고
    • A new low cost magnetic material: Magnetic polyvinylbutyral microbeads
    • Tanyolac D, Ozdural AR: A new low cost magnetic material: magnetic polyvinylbutyral microbeads. React Funct Polym 2000, 43:279-286.
    • (2000) React Funct Polym , vol.43 , pp. 279-286
    • Tanyolac, D.1    Ozdural, A.R.2
  • 12
    • 0000102206 scopus 로고
    • Preparation and characterization of novel magnetite-coated ion-exchange particles
    • Nixon L, Koval CA, Noble RD, Slaff GS: Preparation and characterization of novel magnetite-coated ion-exchange particles. Chem Mater 1992, 4:117-121.
    • (1992) Chem Mater , vol.4 , pp. 117-121
    • Nixon, L.1    Koval, C.A.2    Noble, R.D.3    Slaff, G.S.4
  • 13
    • 0017712133 scopus 로고
    • Magnetic ferrofluids for preparation of magnetic polymers and their application in affinity chromatography
    • Mosbach K, Andersson L: Magnetic ferrofluids for preparation of magnetic polymers and their application in affinity chromatography. Nature 1977, 270:259-261.
    • (1977) Nature , vol.270 , pp. 259-261
    • Mosbach, K.1    Andersson, L.2
  • 14
    • 51249179943 scopus 로고
    • Affinity separation of enzymes from mixtures containing suspended solids. Comparisons of magnetic and nonmagnetic techniques
    • Hirschbein BL, Whitesides GM: Affinity separation of enzymes from mixtures containing suspended solids. Comparisons of magnetic and nonmagnetic techniques. Appl Biochem Biotechnol 1982, 7:157-176.
    • (1982) Appl Biochem Biotechnol , vol.7 , pp. 157-176
    • Hirschbein, B.L.1    Whitesides, G.M.2
  • 15
    • 0035060138 scopus 로고    scopus 로고
    • Preparation and characterization of affinity magnetoliposomes useful for the detection of antiphospholipid antibodies
    • Rocha FM, de Pinho SC, Zollner RL, Santana MHA: Preparation and characterization of affinity magnetoliposomes useful for the detection of antiphospholipid antibodies. J Magn Magn Mater 2001, 225:101-108.
    • (2001) J Magn Magn Mater , vol.225 , pp. 101-108
    • Rocha, F.M.1    De Pinho, S.C.2    Zollner, R.L.3    Santana, M.H.A.4
  • 18
    • 4544229220 scopus 로고    scopus 로고
    • Multicomponent magnetic nanorods for biomolecular separations
    • Lee KB, Park S, Mirkin CA: Multicomponent magnetic nanorods for biomolecular separations. Angew Chem - Int Edit 2004, 43:3048-3050.
    • (2004) Angew Chem - Int Edit , vol.43 , pp. 3048-3050
    • Lee, K.B.1    Park, S.2    Mirkin, C.A.3
  • 19
    • 0035210379 scopus 로고    scopus 로고
    • Large-scale separation of magnetic bioaffinity adsorbents
    • Safarik I, Ptackova L, Safarikova M: Large-scale separation of magnetic bioaffinity adsorbents. Biotechnol Lett 2001, 23:1953-1956.
    • (2001) Biotechnol Lett , vol.23 , pp. 1953-1956
    • Safarik, I.1    Ptackova, L.2    Safarikova, M.3
  • 21
    • 0002992730 scopus 로고
    • Fluidized-bed separators reviewed: A low pressure drop approach to column chromatography
    • Lochmuller CH, Ronsick CS, Wigman LS: Fluidized-bed separators reviewed: a low pressure drop approach to column chromatography. Prep Chromatogr 1988, 1:93-108.
    • (1988) Prep Chromatogr , vol.1 , pp. 93-108
    • Lochmuller, C.H.1    Ronsick, C.S.2    Wigman, L.S.3
  • 22
    • 0022082297 scopus 로고
    • Continuous affinity chromatography using a magnetically stabilized fluidized bed
    • Burns MA, Graves DJ: Continuous affinity chromatography using a magnetically stabilized fluidized bed. Biotechnol Progr 1985, 1:95-103.
    • (1985) Biotechnol Progr , vol.1 , pp. 95-103
    • Burns, M.A.1    Graves, D.J.2
  • 23
    • 0026261942 scopus 로고
    • Continuous protein separations in a magnetically stabilized fluidized bed using nonmagnetic supports
    • Chetty AS, Burns MA: Continuous protein separations in a magnetically stabilized fluidized bed using nonmagnetic supports. Biotechnol Bioeng 1991, 38:963-971.
    • (1991) Biotechnol Bioeng , vol.38 , pp. 963-971
    • Chetty, A.S.1    Burns, M.A.2
  • 24
    • 0023489952 scopus 로고
    • Magnetic aqueous two-phase separation: A new technique to increase rate of phase-separation, using dextran-ferrofluid or larger iron oxide particles
    • Wikstrom P, Flygare S, Grondalen A, Larsson PO: Magnetic aqueous two-phase separation: a new technique to increase rate of phase-separation, using dextran-ferrofluid or larger iron oxide particles. Anal Biochem 1987, 167:331-339.
    • (1987) Anal Biochem , vol.167 , pp. 331-339
    • Wikstrom, P.1    Flygare, S.2    Grondalen, A.3    Larsson, P.O.4
  • 25
    • 0028356642 scopus 로고
    • Magnetically enhanced phase separation
    • Larsson P-O: Magnetically enhanced phase separation. Meth Enzymol 1994, 228:112-117.
    • (1994) Meth Enzymol , vol.228 , pp. 112-117
    • Larsson, P.-O.1
  • 26
    • 0004725966 scopus 로고    scopus 로고
    • Biologically active compounds and xenobiotics: Magnetic affinity separations
    • Edited by: Wilson ID, Adlard RR, Poole CF, Cook MR. London: Academic Press
    • Safarik I, Safarikova M: Biologically active compounds and xenobiotics: Magnetic affinity separations. In Encyclopedia of Separation Science Edited by: Wilson ID, Adlard RR, Poole CF, Cook MR. London: Academic Press; 2000:2163-2170.
    • (2000) Encyclopedia of Separation Science , pp. 2163-2170
    • Safarik, I.1    Safarikova, M.2
  • 27
    • 0002293732 scopus 로고    scopus 로고
    • Overview of magnetic separations used in biochemical and biotechnological applications
    • Edited by: Hafeli U, Schutt W, Teller J, Zborowski M. New York and London: Plenum Press
    • Safarik I, Safarikova M: Overview of magnetic separations used in biochemical and biotechnological applications. In Scientific and Clinical Applications of Magnetic Carriers Edited by: Hafeli U, Schutt W, Teller J, Zborowski M. New York and London: Plenum Press; 1997:323-340.
    • (1997) Scientific and Clinical Applications of Magnetic Carriers , pp. 323-340
    • Safarik, I.1    Safarikova, M.2
  • 28
    • 0000393965 scopus 로고    scopus 로고
    • The application of magnetic techniques in biosciences
    • Safarikova M, Safarik I: The application of magnetic techniques in biosciences. Magn Electr Sep 2001, 10:223-252.
    • (2001) Magn Electr Sep , vol.10 , pp. 223-252
    • Safarikova, M.1    Safarik, I.2
  • 29
    • 6944252020 scopus 로고    scopus 로고
    • Application of magnetic techniques in the field of drug discovery and biomedicine
    • Saiyed ZM, Telang SD, Ramchand CN: Application of magnetic techniques in the field of drug discovery and biomedicine. BioMagn Res Technol 2003, 1:2.
    • (2003) BioMagn Res Technol , vol.1 , pp. 2
    • Saiyed, Z.M.1    Telang, S.D.2    Ramchand, C.N.3
  • 30
    • 0344305798 scopus 로고    scopus 로고
    • Affinity capture of specific DNA-binding proteins for mass spectrometric identification
    • Yaneva M, Tempst P: Affinity capture of specific DNA-binding proteins for mass spectrometric identification. Anal Chem 2003, 75:6437-6448.
    • (2003) Anal Chem , vol.75 , pp. 6437-6448
    • Yaneva, M.1    Tempst, P.2
  • 31
    • 3543044990 scopus 로고    scopus 로고
    • Gold nanoparticles as selective and concentrating probes for samples in MALDI MS analysis
    • Teng CH, Ho KC, Lin YS, Chen YC: Gold nanoparticles as selective and concentrating probes for samples in MALDI MS analysis. Anal Chem 2004, 76:4337-4342.
    • (2004) Anal Chem , vol.76 , pp. 4337-4342
    • Teng, C.H.1    Ho, K.C.2    Lin, Y.S.3    Chen, Y.C.4
  • 32
    • 0032508479 scopus 로고    scopus 로고
    • Affinity capillary electrophoresis: Important application areas and some recent developments
    • Heegaard NHH, Nilsson S, Guzman NA: Affinity capillary electrophoresis: important application areas and some recent developments. J Chromatogr B 1998, 715:29-54.
    • (1998) J Chromatogr B , vol.715 , pp. 29-54
    • Heegaard, N.H.H.1    Nilsson, S.2    Guzman, N.A.3
  • 33
    • 0031259833 scopus 로고    scopus 로고
    • Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins
    • Nilsson J, Stahl S, Lundeberg J, Uhlen M, Nygren PA: Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins. Protein Expr Purif 1997, 11:1-16.
    • (1997) Protein Expr Purif , vol.11 , pp. 1-16
    • Nilsson, J.1    Stahl, S.2    Lundeberg, J.3    Uhlen, M.4    Nygren, P.A.5
  • 34
    • 33751427281 scopus 로고    scopus 로고
    • Finding the right protein purification system
    • Kobs G: Finding the right protein purification system. Cell Notes 2004, 9:2-5.
    • (2004) Cell Notes , vol.9 , pp. 2-5
    • Kobs, G.1
  • 35
    • 0035975923 scopus 로고    scopus 로고
    • Perspectives of immobilized-metal affinity chromatography
    • Gaberc-Porekar V, Menart V: Perspectives of immobilized-metal affinity chromatography. J Biochem Biophys Methods 2001, 49:335-360.
    • (2001) J Biochem Biophys Methods , vol.49 , pp. 335-360
    • Gaberc-Porekar, V.1    Menart, V.2
  • 36
    • 0142091112 scopus 로고    scopus 로고
    • Novel purification system for 6xHis-tagged proteins by magnetic affinity separation
    • Frenzel A, Bergemann C, Kohl G, Reinard T: Novel purification system for 6xHis-tagged proteins by magnetic affinity separation. J Chromatogr B 2003, 793:325-329.
    • (2003) J Chromatogr B , vol.793 , pp. 325-329
    • Frenzel, A.1    Bergemann, C.2    Kohl, G.3    Reinard, T.4
  • 37
    • 0027489618 scopus 로고
    • Comparison of immunomagnetic beads coated with protein A, protein G, or goat anti-mouse immunoglobulins
    • Widjojoatmodjo MN, Fluit AC, Torensma R, Verhoef J: Comparison of immunomagnetic beads coated with protein A, protein G, or goat anti-mouse immunoglobulins. J Immunol Methods 1993, 165:11-19.
    • (1993) J Immunol Methods , vol.165 , pp. 11-19
    • Widjojoatmodjo, M.N.1    Fluit, A.C.2    Torensma, R.3    Verhoef, J.4
  • 40
    • 0035938902 scopus 로고    scopus 로고
    • Plasminogen binds to disease-associated prion protein of multiple species
    • Maissen M, Roeckl F, Glatzel M, Goldmann W, Aguzzi A: Plasminogen binds to disease-associated prion protein of multiple species. Lancet 2001, 357:2026-2028.
    • (2001) Lancet , vol.357 , pp. 2026-2028
    • Maissen, M.1    Roeckl, F.2    Glatzel, M.3    Goldmann, W.4    Aguzzi, A.5
  • 41
    • 0038119665 scopus 로고    scopus 로고
    • Efficient inclusion body processing using chemical extraction and high gradient magnetic fishing
    • Heeboll-Nielsen A, Choe WS, Middelberg APJ, Thomas ORT: Efficient inclusion body processing using chemical extraction and high gradient magnetic fishing. Biotechnol Progr 2003, 19:887-898.
    • (2003) Biotechnol Progr , vol.19 , pp. 887-898
    • Heeboll-Nielsen, A.1    Choe, W.S.2    Middelberg, A.P.J.3    Thomas, O.R.T.4
  • 42
  • 43
    • 31544442057 scopus 로고    scopus 로고
    • Magnetic solid-phase extraction of target analytes from large volumes of urine
    • Safarikova M, Safarik I: Magnetic solid-phase extraction of target analytes from large volumes of urine. Eur Cells Mater 2002, 3(Suppl 2):192-195.
    • (2002) Eur Cells Mater , vol.3 , Issue.SUPPL. 2 , pp. 192-195
    • Safarikova, M.1    Safarik, I.2
  • 44
    • 0028972870 scopus 로고
    • Xenopus lamin B3 has a direct role in the assembly of a replication competent nucleus: Evidence from cell-free egg extracts
    • Goldberg M, Jenkins H, Allen T, Whitfield WG, Hutchison CJ: Xenopus lamin B3 has a direct role in the assembly of a replication competent nucleus: evidence from cell-free egg extracts. J Cell Sci 1995, 108:3451-3461.
    • (1995) J Cell Sci , vol.108 , pp. 3451-3461
    • Goldberg, M.1    Jenkins, H.2    Allen, T.3    Whitfield, W.G.4    Hutchison, C.J.5
  • 45
    • 0031037516 scopus 로고    scopus 로고
    • Prenucleolar bodies contain coilin and are assembled in Xenopus egg extract depleted of specific nucleolar proteins and U3 RNA
    • Bell P, Scheer U: Prenucleolar bodies contain coilin and are assembled in Xenopus egg extract depleted of specific nucleolar proteins and U3 RNA. J Cell Sci 1997, 110:43-54.
    • (1997) J Cell Sci , vol.110 , pp. 43-54
    • Bell, P.1    Scheer, U.2
  • 46
    • 0035063025 scopus 로고    scopus 로고
    • Isolation and removal of proteolytic enzymes with magnetic cross-linked erythrocytes
    • Safarik I, Safarikova M: Isolation and removal of proteolytic enzymes with magnetic cross-linked erythrocytes. J Magn Magn Mater 2001, 225:169-174.
    • (2001) J Magn Magn Mater , vol.225 , pp. 169-174
    • Safarik, I.1    Safarikova, M.2
  • 47
    • 0029101559 scopus 로고
    • Identification of major proteins associated with Dictyostelium discoideum endocytic vesicles
    • Adessi C, Chapel A, Vincon M, Rabilloud T, Klein G, Satre M, Garin J: Identification of major proteins associated with Dictyostelium discoideum endocytic vesicles. J Cell Sci 1995, 108:3331-3337.
    • (1995) J Cell Sci , vol.108 , pp. 3331-3337
    • Adessi, C.1    Chapel, A.2    Vincon, M.3    Rabilloud, T.4    Klein, G.5    Satre, M.6    Garin, J.7
  • 48
    • 0031593684 scopus 로고    scopus 로고
    • Immuno-isolation of highly purified peroxisomes using magnetic beads and continuous immunomagnetic sorting
    • Luers GH, Hartig R, Mohr H, Hausmann M, Fahimi HD, Cremer C, Volkl A: Immuno-isolation of highly purified peroxisomes using magnetic beads and continuous immunomagnetic sorting. Electrophoresis 1998, 19:1205-1210.
    • (1998) Electrophoresis , vol.19 , pp. 1205-1210
    • Luers, G.H.1    Hartig, R.2    Mohr, H.3    Hausmann, M.4    Fahimi, H.D.5    Cremer, C.6    Volkl, A.7
  • 50
    • 0037026235 scopus 로고    scopus 로고
    • High-gradient magnetic affinity separation of trypsin from porcine pancreatin
    • Hubbuch JJ, Thomas ORT: High-gradient magnetic affinity separation of trypsin from porcine pancreatin. Biotechnol Bioeng 2002, 79:301-313.
    • (2002) Biotechnol Bioeng , vol.79 , pp. 301-313
    • Hubbuch, J.J.1    Thomas, O.R.T.2
  • 52
    • 0035128695 scopus 로고    scopus 로고
    • A novel magnetic affinity support for protein adsorption and purification
    • Tong XD, Xue B, Sun Y: A novel magnetic affinity support for protein adsorption and purification. Biotechnol Progr 2001, 17:134-139.
    • (2001) Biotechnol Progr , vol.17 , pp. 134-139
    • Tong, X.D.1    Xue, B.2    Sun, Y.3
  • 54
    • 0036006044 scopus 로고    scopus 로고
    • Identification, purification, and molecular cloning of N-1-naphthylphthalmic acid-binding plasma membrane-associated aminopeptidases from Arabidopsis
    • Murphy AS, Hoogner KR, Peer WA, Taiz L: Identification, purification, and molecular cloning of N-1-naphthylphthalmic acid-binding plasma membrane-associated aminopeptidases from Arabidopsis. Plant Physiol 2002, 128:935-950.
    • (2002) Plant Physiol , vol.128 , pp. 935-950
    • Murphy, A.S.1    Hoogner, K.R.2    Peer, W.A.3    Taiz, L.4
  • 55
    • 0036198007 scopus 로고    scopus 로고
    • Magnetite-alginate beads for purification of some starch degrading enzymes
    • Teotia S, Gupta MN: Magnetite-alginate beads for purification of some starch degrading enzymes. Mol Biotechnol 2002, 20:231-237.
    • (2002) Mol Biotechnol , vol.20 , pp. 231-237
    • Teotia, S.1    Gupta, M.N.2
  • 56
    • 0032488934 scopus 로고    scopus 로고
    • Preparation of magnetic immobilized metal affinity separation media and its use in the isolation of proteins
    • Abudiab T, Beitle RR: Preparation of magnetic immobilized metal affinity separation media and its use in the isolation of proteins. J Chromatogr A 1998, 795:211-217.
    • (1998) J Chromatogr A , vol.795 , pp. 211-217
    • Abudiab, T.1    Beitle, R.R.2
  • 57
    • 0027939095 scopus 로고
    • Immunoseparation of membrane peptidases from pig lung membranes using magnetic beads
    • Barnes K, Murphy LJ, Turner AJ: Immunoseparation of membrane peptidases from pig lung membranes using magnetic beads. Biochem Soc Trans 1994, 22:S451-S451.
    • (1994) Biochem Soc Trans , vol.22
    • Barnes, K.1    Murphy, L.J.2    Turner, A.J.3
  • 58
    • 0016215576 scopus 로고
    • Purification of enzymes using magnetic bioaffinity materials
    • Dunnill P, Lilly MD: Purification of enzymes using magnetic bioaffinity materials. Biotechnol Bioeng 1974, 16:987-990.
    • (1974) Biotechnol Bioeng , vol.16 , pp. 987-990
    • Dunnill, P.1    Lilly, M.D.2
  • 59
    • 4344695074 scopus 로고    scopus 로고
    • Fast separation of bromelain by polyacrylic acid-bound iron oxide magnetic nanoparticles
    • Chen D-H, Huang S-H: Fast separation of bromelain by polyacrylic acid-bound iron oxide magnetic nanoparticles. Process Biochem 2004, 39:2207-2211.
    • (2004) Process Biochem , vol.39 , pp. 2207-2211
    • Chen, D.-H.1    Huang, S.-H.2
  • 60
    • 0036624845 scopus 로고    scopus 로고
    • Characterization of caspase-8L: A novel isoform of caspase-8 that behaves as an inhibitor of the caspase cascade
    • Himeji D, Horiuchi T, Tsukamoto H, Hayashi K, Watanabe T, Harada M: Characterization of caspase-8L: a novel isoform of caspase-8 that behaves as an inhibitor of the caspase cascade. Blood 2002, 99:4070-4078.
    • (2002) Blood , vol.99 , pp. 4070-4078
    • Himeji, D.1    Horiuchi, T.2    Tsukamoto, H.3    Hayashi, K.4    Watanabe, T.5    Harada, M.6
  • 61
    • 1842418655 scopus 로고    scopus 로고
    • Novel metal-chelate affinity sorbents for reversible use in catalase adsorption
    • Akgol S, Denizli A: Novel metal-chelate affinity sorbents for reversible use in catalase adsorption. J Mol Catal B - Enzym 2004, 28:7-14.
    • (2004) J Mol Catal B - Enzym , vol.28 , pp. 7-14
    • Akgol, S.1    Denizli, A.2
  • 62
    • 0029132518 scopus 로고
    • Preparation of trypsin free chymotrypsin
    • Ghosh M, Tyagi R, Gupta MN: Preparation of trypsin free chymotrypsin. Biotechnol Tech 1995, 9:149-152.
    • (1995) Biotechnol Tech , vol.9 , pp. 149-152
    • Ghosh, M.1    Tyagi, R.2    Gupta, M.N.3
  • 63
    • 0030582401 scopus 로고    scopus 로고
    • Non-porous magnetic chelator supports for protein recovery by immobilised metal affinity adsorption
    • O'Brien SM, Thomas ORT, Dunnill P: Non-porous magnetic chelator supports for protein recovery by immobilised metal affinity adsorption. J Biotechnol 1996, 50:13-25.
    • (1996) J Biotechnol , vol.50 , pp. 13-25
    • O'Brien, S.M.1    Thomas, O.R.T.2    Dunnill, P.3
  • 64
    • 0027462338 scopus 로고
    • Immobilization and recovery of fusion proteins and B-lymphocyte cells using magnetic separation
    • Ljungquist C, Lundeberg J, Rasmussen AM, Hornes E, Uhlen M: Immobilization and recovery of fusion proteins and B-lymphocyte cells using magnetic separation. DNA Cell Biol 1993, 12:191-197.
    • (1993) DNA Cell Biol , vol.12 , pp. 191-197
    • Ljungquist, C.1    Lundeberg, J.2    Rasmussen, A.M.3    Hornes, E.4    Uhlen, M.5
  • 65
    • 0019768807 scopus 로고
    • Magnetic biospecific affinity adsorbents for immunoglobulin and enzyme isolation
    • Griffin T, Mosbach K, Mosbach R: Magnetic biospecific affinity adsorbents for immunoglobulin and enzyme isolation. Appl Biochem Biotechnol 1981, 6:283-292.
    • (1981) Appl Biochem Biotechnol , vol.6 , pp. 283-292
    • Griffin, T.1    Mosbach, K.2    Mosbach, R.3
  • 66
    • 0026210091 scopus 로고
    • A magnetizable solid phase for enzyme extraction
    • Ennis MP, Wisdom GB: A magnetizable solid phase for enzyme extraction. Appl Biochem Biotechnol 1991, 30:155-164.
    • (1991) Appl Biochem Biotechnol , vol.30 , pp. 155-164
    • Ennis, M.P.1    Wisdom, G.B.2
  • 69
    • 33751407097 scopus 로고    scopus 로고
    • Efficient purification of His-tagged proteins from insect and mammalian cells
    • Betz N: Efficient purification of His-tagged proteins from insect and mammalian cells. Promega Notes 2004, 87:29-32.
    • (2004) Promega Notes , vol.87 , pp. 29-32
    • Betz, N.1
  • 70
    • 33751423224 scopus 로고    scopus 로고
    • Purifying His-tagged proteins from insect and mammalian cells
    • Betz N: Purifying His-tagged proteins from insect and mammalian cells. Cell Notes 2004, 9:6-9.
    • (2004) Cell Notes , vol.9 , pp. 6-9
    • Betz, N.1
  • 71
    • 0343951804 scopus 로고
    • Magnetic biospecific affinity adsorbents for lysozyme isolation
    • Safarik I: Magnetic biospecific affinity adsorbents for lysozyme isolation. Biotechnol Tech 1991, 5:111-114.
    • (1991) Biotechnol Tech , vol.5 , pp. 111-114
    • Safarik, I.1
  • 72
    • 2542609192 scopus 로고    scopus 로고
    • Cibacron blue F3GA incorporated magnetic poly(2-hydroxyethyl methacrylate) beads for lysozyme adsorption
    • Odabasi M, Denizli A: Cibacron blue F3GA incorporated magnetic poly(2-hydroxyethyl methacrylate) beads for lysozyme adsorption. J Appl Polym Sci 2004, 93:719-725.
    • (2004) J Appl Polym Sci , vol.93 , pp. 719-725
    • Odabasi, M.1    Denizli, A.2
  • 73
    • 0028836676 scopus 로고
    • Axial dispersion in liquid magnetically stabilized fluidized beds
    • Goto M, Imamura T, Hirose T: Axial dispersion in liquid magnetically stabilized fluidized beds. J Chromatogr A 1995, 690:1-8.
    • (1995) J Chromatogr A , vol.690 , pp. 1-8
    • Goto, M.1    Imamura, T.2    Hirose, T.3
  • 74
    • 0344069728 scopus 로고    scopus 로고
    • Purification and characterization of the lysozyme from the gut of the soft tick Ornithodoros moubata
    • Kopacek P, Vogt R, Jindrak L, Weise C, Safarik I: Purification and characterization of the lysozyme from the gut of the soft tick Ornithodoros moubata. Insect Biochem Mol Biol 1999, 29:989-997.
    • (1999) Insect Biochem Mol Biol , vol.29 , pp. 989-997
    • Kopacek, P.1    Vogt, R.2    Jindrak, L.3    Weise, C.4    Safarik, I.5
  • 75
    • 0036858665 scopus 로고    scopus 로고
    • Fast and efficient adsorption/desorption of protein by a novel magnetic nano-adsorbent
    • Liao MH, Chen DH: Fast and efficient adsorption/desorption of protein by a novel magnetic nano-adsorbent. Biotechnol Lett 2002, 24:1913-1917.
    • (2002) Biotechnol Lett , vol.24 , pp. 1913-1917
    • Liao, M.H.1    Chen, D.H.2
  • 76
    • 0035816454 scopus 로고    scopus 로고
    • Protein adsorption equilibria and kinetics to a poly(vinyl alcohol)-based magnetic affinity support
    • Xue B, Sun Y: Protein adsorption equilibria and kinetics to a poly(vinyl alcohol)-based magnetic affinity support. J Chromatogr A 2001, 921:109-119.
    • (2001) J Chromatogr A , vol.921 , pp. 109-119
    • Xue, B.1    Sun, Y.2
  • 77
    • 0347413687 scopus 로고    scopus 로고
    • Application of magnetic agarose support in liquid magnetically stabilized fluidized bed for protein adsorption
    • Tong XD, Sun Y: Application of magnetic agarose support in liquid magnetically stabilized fluidized bed for protein adsorption. Biotechnol Progr 2003, 19:1721-1727.
    • (2003) Biotechnol Progr , vol.19 , pp. 1721-1727
    • Tong, X.D.1    Sun, Y.2
  • 78
    • 24044550771 scopus 로고    scopus 로고
    • The preparation of chitosan affinity magnetic nanoparticles and their adsorption properties for proteins
    • Yu YH, Xue B, Sun Y, He BL: The preparation of chitosan affinity magnetic nanoparticles and their adsorption properties for proteins. Acta Polym Sinica 2000:340-344.
    • (2000) Acta Polym Sinica , pp. 340-344
    • Yu, Y.H.1    Xue, B.2    Sun, Y.3    He, B.L.4
  • 79
    • 18144431694 scopus 로고    scopus 로고
    • Ferrofluid-modified plant-based materials as adsorbents for batch separation of selected biologically active compounds and xenobiotics
    • in press
    • Safarik I, Safarikova M, Weyda F, Mosiniewicz-Szablewska W, Slawska-Waniewska A: Ferrofluid-modified plant-based materials as adsorbents for batch separation of selected biologically active compounds and xenobiotics. J Magn Magn Mater in press.
    • J Magn Magn Mater
    • Safarik, I.1    Safarikova, M.2    Weyda, F.3    Mosiniewicz-Szablewska, W.4    Slawska-Waniewska, A.5
  • 80
    • 2542445177 scopus 로고    scopus 로고
    • Adsorption and desorption of lysozyme on nano-sized magnetic particles and its conformational changes
    • Peng ZG, Hidajat K, Uddin MS: Adsorption and desorption of lysozyme on nano-sized magnetic particles and its conformational changes. Colloid Surf B - Biointerfaces 2004, 35:169-174.
    • (2004) Colloid Surf B - Biointerfaces , vol.35 , pp. 169-174
    • Peng, Z.G.1    Hidajat, K.2    Uddin, M.S.3
  • 81
    • 0030615948 scopus 로고    scopus 로고
    • Characterisation of non-porous magnetic chelator supports and their use to recover polyhistidine-tailed T4 lysozyme from a crude E. coli extract
    • O'Brien SM, Sloane RP, Thomas ORT, Dunnill P: Characterisation of non-porous magnetic chelator supports and their use to recover polyhistidine-tailed T4 lysozyme from a crude E. coli extract. J Biotechnol 1997, 54:53-67.
    • (1997) J Biotechnol , vol.54 , pp. 53-67
    • O'Brien, S.M.1    Sloane, R.P.2    Thomas, O.R.T.3    Dunnill, P.4
  • 82
    • 0028894603 scopus 로고
    • Purification and immobilization of Aspergillus niger pectinase on magnetic latex beads
    • Tyagi R, Gupta MN: Purification and immobilization of Aspergillus niger pectinase on magnetic latex beads. Biocatal Biotransform 1995, 12:293-298.
    • (1995) Biocatal Biotransform , vol.12 , pp. 293-298
    • Tyagi, R.1    Gupta, M.N.2
  • 84
    • 0035543890 scopus 로고    scopus 로고
    • High gradient magnetic separation versus expanded bed adsorption: A first principle comparison
    • Hubbuch JJ, Matthiesen DB, Hobley TJ, Thomas ORT: High gradient magnetic separation versus expanded bed adsorption: a first principle comparison. Bioseparation 2001, 10:99-112.
    • (2001) Bioseparation , vol.10 , pp. 99-112
    • Hubbuch, J.J.1    Matthiesen, D.B.2    Hobley, T.J.3    Thomas, O.R.T.4
  • 85
    • 33751412659 scopus 로고    scopus 로고
    • Rapid detection and quantitation of His-tagged proteins purified by MagneHis™ Ni-particles
    • Engel L, Kar S, Johnson T: Rapid detection and quantitation of His-tagged proteins purified by MagneHis™ Ni-particles. Promega Notes 2003, 84:27-30.
    • (2003) Promega Notes , vol.84 , pp. 27-30
    • Engel, L.1    Kar, S.2    Johnson, T.3
  • 86
    • 0000182447 scopus 로고    scopus 로고
    • The synthesis of sub-micron magnetic particles and their use for preparative purification of proteins
    • Khng HP, Cunliffe D, Davies S, Turner NA, Vulfson EN: The synthesis of sub-micron magnetic particles and their use for preparative purification of proteins. Biotechnol Bioeng 1998, 60:419-424.
    • (1998) Biotechnol Bioeng , vol.60 , pp. 419-424
    • Khng, H.P.1    Cunliffe, D.2    Davies, S.3    Turner, N.A.4    Vulfson, E.N.5
  • 87
    • 0018342612 scopus 로고
    • Recovery of free enzymes from product liquors by bio-affinity adsorption: Trypsin binding by immobilised soybean inhibitor
    • Halling PJ, Dunnill P: Recovery of free enzymes from product liquors by bio-affinity adsorption: Trypsin binding by immobilised soybean inhibitor. European J Appl Microbiol 1979, 6:195-205.
    • (1979) European J Appl Microbiol , vol.6 , pp. 195-205
    • Halling, P.J.1    Dunnill, P.2
  • 88
    • 0023456768 scopus 로고
    • Affinity separations in magnetically stabilized fluidized beds. Synthesis and performance of packing materials
    • Lochmuller CH, Wigman LS: Affinity separations in magnetically stabilized fluidized beds. Synthesis and performance of packing materials. Sep Sci Technol 1987, 22:2111-2125.
    • (1987) Sep Sci Technol , vol.22 , pp. 2111-2125
    • Lochmuller, C.H.1    Wigman, L.S.2
  • 89
    • 0023558763 scopus 로고
    • Aerosol-jet produced, magnetic carrageenan-gel particles: A new affinity chromatography matrix
    • Lochmuller CH, Wigman LS, Kitchell BS: Aerosol-jet produced, magnetic carrageenan-gel particles: a new affinity chromatography matrix. J Chem Technol Biotechnol 1987, 40:33-40.
    • (1987) J Chem Technol Biotechnol , vol.40 , pp. 33-40
    • Lochmuller, C.H.1    Wigman, L.S.2    Kitchell, B.S.3
  • 90
    • 0031553515 scopus 로고    scopus 로고
    • Preparation of magnetically susceptible polyacrylamide/magnetite beads for use in magnetically stabilized fluidized bed chromatography
    • Cocker TM, Fee CJ, Evans RA: Preparation of magnetically susceptible polyacrylamide/magnetite beads for use in magnetically stabilized fluidized bed chromatography. Biotechnol Bioeng 1997, 53:79-87.
    • (1997) Biotechnol Bioeng , vol.53 , pp. 79-87
    • Cocker, T.M.1    Fee, C.J.2    Evans, R.A.3
  • 91
    • 0035427612 scopus 로고    scopus 로고
    • Characterization and application of high magnetic property chitosan particles
    • An XN, Su ZX: Characterization and application of high magnetic property chitosan particles. J Appl Polym Sci 2001, 81:1175-1181.
    • (2001) J Appl Polym Sci , vol.81 , pp. 1175-1181
    • An, X.N.1    Su, Z.X.2
  • 92
    • 0036413508 scopus 로고    scopus 로고
    • A purification method of the diagnostic enzyme Bacillus uricase using magnetic beads and nonspecific protease
    • Nishiya Y, Hibi T, Oda JL: A purification method of the diagnostic enzyme Bacillus uricase using magnetic beads and nonspecific protease. Protein Expr Purif 2002, 25:426-429.
    • (2002) Protein Expr Purif , vol.25 , pp. 426-429
    • Nishiya, Y.1    Hibi, T.2    Oda, J.L.3
  • 93
    • 0347268311 scopus 로고    scopus 로고
    • Preparation of novel magnetic affinity adsorbents and application for purification of urokinase
    • Dong YS, Liang F, Jin HX, Xi Q, Chang JH: Preparation of novel magnetic affinity adsorbents and application for purification of urokinase. Chem J Chin Univ - Chin 2002, 23:1013-1017.
    • (2002) Chem J Chin Univ - Chin , vol.23 , pp. 1013-1017
    • Dong, Y.S.1    Liang, F.2    Jin, H.X.3    Xi, Q.4    Chang, J.H.5
  • 94
    • 0035385951 scopus 로고    scopus 로고
    • The use of derivatized magnetoliposomes for extraction of antibodies from aqueous solutions
    • Dumitrascu G, Kumbhar A, Zhou WL, Rosenzweig Z: The use of derivatized magnetoliposomes for extraction of antibodies from aqueous solutions. IEEE Trans Magn 2001, 37:2932-2934.
    • (2001) IEEE Trans Magn , vol.37 , pp. 2932-2934
    • Dumitrascu, G.1    Kumbhar, A.2    Zhou, W.L.3    Rosenzweig, Z.4
  • 95
    • 0035949202 scopus 로고    scopus 로고
    • Polyhydroxyethylmethacrylate-based magnetic DNA-affinity beads for anti-DNA antibody removal from systemic lupus erythematosus patient plasma
    • Odabasi M, Denizli A: Polyhydroxyethylmethacrylate-based magnetic DNA-affinity beads for anti-DNA antibody removal from systemic lupus erythematosus patient plasma. J Chromatogr B 2001, 760:137-148.
    • (2001) J Chromatogr B , vol.760 , pp. 137-148
    • Odabasi, M.1    Denizli, A.2
  • 96
    • 2842606888 scopus 로고    scopus 로고
    • Preparation and application of magnetic affinity adsorbent based on magnetic cellulose bead
    • Li X, Li CX, He BL: Preparation and application of magnetic affinity adsorbent based on magnetic cellulose bead. Chem J Chin Univ - Chin 1998, 19:994-999.
    • (1998) Chem J Chin Univ - Chin , vol.19 , pp. 994-999
    • Li, X.1    Li, C.X.2    He, B.L.3
  • 97
    • 0034646622 scopus 로고    scopus 로고
    • Magnetic bead purification as a rapid and efficient method for enhanced antibody specificity for plant sample immunoblotting and immunolocalization
    • Quitadamo IJ, Kostman TA, Schelling ME, Franceschi VR: Magnetic bead purification as a rapid and efficient method for enhanced antibody specificity for plant sample immunoblotting and immunolocalization. Plant Sci 2000, 153:7-14.
    • (2000) Plant Sci , vol.153 , pp. 7-14
    • Quitadamo, I.J.1    Kostman, T.A.2    Schelling, M.E.3    Franceschi, V.R.4
  • 98
    • 0005803671 scopus 로고
    • Rapid purification of monoclonal antibody with functional magnetite particles
    • Shinkai M, Kamihira M, Honda H, Kobayashi T: Rapid purification of monoclonal antibody with functional magnetite particles. Kag Kog Ronbunshu 1992, 18:256-259.
    • (1992) Kag Kog Ronbunshu , vol.18 , pp. 256-259
    • Shinkai, M.1    Kamihira, M.2    Honda, H.3    Kobayashi, T.4
  • 99
    • 0028281908 scopus 로고
    • Development and application of thermo-sensitive magnetic immunomicrospheres for antibody purification
    • Kondo A, Kamura H, Higashitani K: Development and application of thermo-sensitive magnetic immunomicrospheres for antibody purification. Appl Microbiol Biotechnol 1994, 41:99-105.
    • (1994) Appl Microbiol Biotechnol , vol.41 , pp. 99-105
    • Kondo, A.1    Kamura, H.2    Higashitani, K.3
  • 100
    • 4043149229 scopus 로고    scopus 로고
    • A novel magnetic adsorbent for immunoglobulin-G purification in a magnetically stabilized fluidized bed
    • Ozkara S, Akgol S, Canak Y, Denizli A: A novel magnetic adsorbent for immunoglobulin-G purification in a magnetically stabilized fluidized bed. Biotechnol Progress 2004, 20:1169-1175.
    • (2004) Biotechnol Progress , vol.20 , pp. 1169-1175
    • Ozkara, S.1    Akgol, S.2    Canak, Y.3    Denizli, A.4
  • 101
    • 2342541640 scopus 로고    scopus 로고
    • Cloning and expression of fused Fc-binding protein (SPA-SPG) and its application in purification of IgG
    • Meng ZH, Lin B, Xie YH, Zhang KQ: Cloning and expression of fused Fc-binding protein (SPA-SPG) and its application in purification of IgG. Progr Biochem Biophys 2004, 31:146-149.
    • (2004) Progr Biochem Biophys , vol.31 , pp. 146-149
    • Meng, Z.H.1    Lin, B.2    Xie, Y.H.3    Zhang, K.Q.4
  • 102
    • 0031805733 scopus 로고    scopus 로고
    • Efficient purification of mouse anti-FGF receptor IgM monoclonal antibody by magnetic beads
    • Quitadamo IJ, Schelling ME: Efficient purification of mouse anti-FGF receptor IgM monoclonal antibody by magnetic beads. Hybridoma 1998, 17:199-207.
    • (1998) Hybridoma , vol.17 , pp. 199-207
    • Quitadamo, I.J.1    Schelling, M.E.2
  • 103
    • 0030296718 scopus 로고    scopus 로고
    • Identification of two nuclear proteins which bind to RNA CUG repeats: Significance for myotonic dystrophy
    • Bhagwati S, Ghatpande A, Leung B: Identification of two nuclear proteins which bind to RNA CUG repeats: Significance for myotonic dystrophy. Biochem Biophys Res Commun 1996, 228:55-62.
    • (1996) Biochem Biophys Res Commun , vol.228 , pp. 55-62
    • Bhagwati, S.1    Ghatpande, A.2    Leung, B.3
  • 104
    • 0024319092 scopus 로고
    • Magnetic DNA affinity purification of yeast transcription factor τ - A new purification principle for the ultrarapid isolation of near homogeneous factor
    • Gabrielsen OS, Hornes E, Korsnes L, Ruet A, Oyen TB: Magnetic DNA affinity purification of yeast transcription factor τ - a new purification principle for the ultrarapid isolation of near homogeneous factor. Nucleic Acids Res 1989, 17:6253-6267.
    • (1989) Nucleic Acids Res , vol.17 , pp. 6253-6267
    • Gabrielsen, O.S.1    Hornes, E.2    Korsnes, L.3    Ruet, A.4    Oyen, T.B.5
  • 105
    • 0027259433 scopus 로고
    • Magnetic DNA affinity purification of yeast transcription factor
    • Gabrielsen OS, Huet J: Magnetic DNA affinity purification of yeast transcription factor. Meth Enzymol 1993, 218:508-525.
    • (1993) Meth Enzymol , vol.218 , pp. 508-525
    • Gabrielsen, O.S.1    Huet, J.2
  • 106
    • 0028088525 scopus 로고
    • Enrichment of DNA-binding proteins from crude tissue for electrophoretic mobility shift assay using magnetic phospho cellulose particles
    • Hollung K, Gabrielsen OS, Jakobsen KS: Enrichment of DNA-binding proteins from crude tissue for electrophoretic mobility shift assay using magnetic phospho cellulose particles. Nucleic Acids Res 1994, 22:3261-3262.
    • (1994) Nucleic Acids Res , vol.22 , pp. 3261-3262
    • Hollung, K.1    Gabrielsen, O.S.2    Jakobsen, K.S.3
  • 107
    • 0029310476 scopus 로고
    • One-step magnetic purification of recombinant DNA-binding proteins using magnetizable phosphocellulose
    • Risoen PA, Struksnes K, Myrset AH, Gabrielsen OS: One-step magnetic purification of recombinant DNA-binding proteins using magnetizable phosphocellulose. Protein Expr Purif 1995, 6:272-277.
    • (1995) Protein Expr Purif , vol.6 , pp. 272-277
    • Risoen, P.A.1    Struksnes, K.2    Myrset, A.H.3    Gabrielsen, O.S.4
  • 108
    • 0037415120 scopus 로고    scopus 로고
    • Characterization of the 5′-flanking fragment of the human GM3-synthase gene
    • Zeng GC, Gao LY, Xia T, Tencomnao T, Yu RK: Characterization of the 5′-flanking fragment of the human GM3-synthase gene. Biochim Biophys Acta 2003, 1625:30-35.
    • (2003) Biochim Biophys Acta , vol.1625 , pp. 30-35
    • Zeng, G.C.1    Gao, L.Y.2    Xia, T.3    Tencomnao, T.4    Yu, R.K.5
  • 109
    • 0025362256 scopus 로고
    • Early transcription factor subunits are encoded by vaccinia virus late genes
    • Gershon PD, Moss B: Early transcription factor subunits are encoded by vaccinia virus late genes. Proc Natl Acad Sci USA 1990, 87:4401-4405.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4401-4405
    • Gershon, P.D.1    Moss, B.2
  • 111
    • 33751420401 scopus 로고    scopus 로고
    • Rapid purification of a prokaryotic regulatory protein with μ MACS™ Streptavidin MicroBeads
    • Kalivoda KA, Braun KW, Vimr ER: Rapid purification of a prokaryotic regulatory protein with μ MACS™ Streptavidin MicroBeads. MACS&more 2003, 7:8-9.
    • (2003) MACS&more , vol.7 , pp. 8-9
    • Kalivoda, K.A.1    Braun, K.W.2    Vimr, E.R.3
  • 112
    • 0027522214 scopus 로고
    • Purification and characterization of p27, a protein from hepatocyte chromatin. Evidence suggesting that it binds selectively to guanine-rich single-stranded DNA
    • Rahat MA, Fry M: Purification and characterization of p27, a protein from hepatocyte chromatin. Evidence suggesting that it binds selectively to guanine-rich single-stranded DNA. FEBS Lett 1993, 334:60-64.
    • (1993) FEBS Lett , vol.334 , pp. 60-64
    • Rahat, M.A.1    Fry, M.2
  • 113
    • 0035844150 scopus 로고    scopus 로고
    • Systematic evolution of a DNA aptamer binding to rat brain tumor microvessels. Selective targeting of endothelial regulatory protein pigpen
    • Blank M, Weinschenk T, Priemer M, Schluesener H: Systematic evolution of a DNA aptamer binding to rat brain tumor microvessels. Selective targeting of endothelial regulatory protein pigpen. J Biol Chem 2001, 276:16464-16468.
    • (2001) J Biol Chem , vol.276 , pp. 16464-16468
    • Blank, M.1    Weinschenk, T.2    Priemer, M.3    Schluesener, H.4
  • 114
    • 6944254390 scopus 로고    scopus 로고
    • Isolation of mRNA binding proteins using the μ MACS streptavidin kit
    • Albig A: Isolation of mRNA binding proteins using the μ MACS streptavidin kit. MACS&more 2001, 5:6-7.
    • (2001) MACS&more , vol.5 , pp. 6-7
    • Albig, A.1
  • 115
    • 0026607355 scopus 로고
    • A protein which specifically binds to single stranded TTAGGGn repeats
    • McKay SJ, Cooke H: A protein which specifically binds to single stranded TTAGGGn repeats. Nucleic Acids Res 1992, 20:1387-1391.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1387-1391
    • McKay, S.J.1    Cooke, H.2
  • 116
    • 0029796380 scopus 로고    scopus 로고
    • Granulocyte colony-stimulating factor activation of Stat3a and Stat3β in immature normal and leukemic human myeloid cells
    • Chakraborty A, White SM, Schaefer TS, Ball ED, Dyer KF, Tweardy DJ: Granulocyte colony-stimulating factor activation of Stat3a and Stat3β in immature normal and leukemic human myeloid cells. Blood 1996, 88:2442-2449.
    • (1996) Blood , vol.88 , pp. 2442-2449
    • Chakraborty, A.1    White, S.M.2    Schaefer, T.S.3    Ball, E.D.4    Dyer, K.F.5    Tweardy, D.J.6
  • 117
    • 0029050226 scopus 로고
    • Ligand-dependent and ligand-independent activation of the transcription factor γRf-1 in a cell-free system
    • Feghali CA, Wright TM: Ligand-dependent and ligand-independent activation of the transcription factor γRf-1 in a cell-free system. Biochem J 1995, 310:461-467.
    • (1995) Biochem J , vol.310 , pp. 461-467
    • Feghali, C.A.1    Wright, T.M.2
  • 118
    • 0028197690 scopus 로고
    • Tethered bandshift assay and affinity purification of a new DNA-binding protein
    • Ren LF, Chen H, Sternberg EA: Tethered bandshift assay and affinity purification of a new DNA-binding protein. Biotechniques 1994, 16:852-855.
    • (1994) Biotechniques , vol.16 , pp. 852-855
    • Ren, L.F.1    Chen, H.2    Sternberg, E.A.3
  • 119
    • 0031656076 scopus 로고    scopus 로고
    • Association of guide RNA binding protein gBP21 with active RNA editing complexes in Trypanosoma brucei
    • Allen TE, Heidmann S, Reed R, Myler PJ, Goringer HU, Stuart KD: Association of guide RNA binding protein gBP21 with active RNA editing complexes in Trypanosoma brucei. Mol Cell Biol 1998, 18:6014-6022.
    • (1998) Mol Cell Biol , vol.18 , pp. 6014-6022
    • Allen, T.E.1    Heidmann, S.2    Reed, R.3    Myler, P.J.4    Goringer, H.U.5    Stuart, K.D.6
  • 120
    • 0034888741 scopus 로고    scopus 로고
    • Isolation of proteins comprising native gene-specific messenger ribonucleoprotein particles using paramagnetic beads
    • Honys D: Isolation of proteins comprising native gene-specific messenger ribonucleoprotein particles using paramagnetic beads. Plant Sci 2001, 161:605-611.
    • (2001) Plant Sci , vol.161 , pp. 605-611
    • Honys, D.1
  • 122
    • 0040143457 scopus 로고    scopus 로고
    • Molecular interactions between single-stranded DNA-binding proteins associated with an essential MCAT element in the mouse smooth muscle alpha-actin promoter
    • Kelm RJ Jr, Cogan JG, Elder PK, Strauch AR, Getz MJ: Molecular interactions between single-stranded DNA-binding proteins associated with an essential MCAT element in the mouse smooth muscle alpha-actin promoter. J Biol Chem 1999, 274:14238-14245.
    • (1999) J Biol Chem , vol.274 , pp. 14238-14245
    • Kelm Jr., R.J.1    Cogan, J.G.2    Elder, P.K.3    Strauch, A.R.4    Getz, M.J.5
  • 123
    • 0347364648 scopus 로고    scopus 로고
    • A tenascin-C aptamer identified by tumor cell SELEX: Systematic evolution of ligands by exponential enrichment
    • Daniels DA, Chen H, Hicke BJ, Swiderek KM, Gold L: A tenascin-C aptamer identified by tumor cell SELEX: Systematic evolution of ligands by exponential enrichment. Proc Natl Acad Sci USA 2003, 100:15416-15421.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15416-15421
    • Daniels, D.A.1    Chen, H.2    Hicke, B.J.3    Swiderek, K.M.4    Gold, L.5
  • 124
    • 0037032989 scopus 로고    scopus 로고
    • Novel target sequences for Pax-6 in the brain-specific activating regions of the rat aldolase C gene
    • Skala-Rubinson H, Vinh J, Labas V, Kahn A, Tuy FPD: Novel target sequences for Pax-6 in the brain-specific activating regions of the rat aldolase C gene. J Biol Chem 2002, 277:47190-47196.
    • (2002) J Biol Chem , vol.277 , pp. 47190-47196
    • Skala-Rubinson, H.1    Vinh, J.2    Labas, V.3    Kahn, A.4    Tuy, F.P.D.5
  • 125
    • 1042296535 scopus 로고    scopus 로고
    • An improved method for the in vitro evolution of aptamers and applications in protein detection and purification
    • Murphy MB, Fuller ST, Richardson PM, Doyle SA: An improved method for the in vitro evolution of aptamers and applications in protein detection and purification. Nucleic Acids Res 2003, 31:e110.
    • (2003) Nucleic Acids Res , vol.31
    • Murphy, M.B.1    Fuller, S.T.2    Richardson, P.M.3    Doyle, S.A.4
  • 126
    • 0034879169 scopus 로고    scopus 로고
    • Agar-based magnetic affinity support for protein adsorption
    • Tong XD, Sun Y: Agar-based magnetic affinity support for protein adsorption. Biotechnol Progr 2001, 17:738-743.
    • (2001) Biotechnol Progr , vol.17 , pp. 738-743
    • Tong, X.D.1    Sun, Y.2
  • 127
    • 0035711592 scopus 로고    scopus 로고
    • Characterization of PVA-based magnetic affinity support for protein adsorption
    • Xue B, Tong XD, Sun Y: Characterization of PVA-based magnetic affinity support for protein adsorption. Sep Sci Technol 2001, 36:2449-2461.
    • (2001) Sep Sci Technol , vol.36 , pp. 2449-2461
    • Xue, B.1    Tong, X.D.2    Sun, Y.3
  • 128
    • 0037154654 scopus 로고    scopus 로고
    • Fabrication and characterization of a rigid magnetic matrix for protein adsorption
    • Xue B, Sun Y: Fabrication and characterization of a rigid magnetic matrix for protein adsorption. J Chromatogr A 2002, 947:185-193.
    • (2002) J Chromatogr A , vol.947 , pp. 185-193
    • Xue, B.1    Sun, Y.2
  • 129
    • 4344628915 scopus 로고    scopus 로고
    • Cu(II)-incorporated, histidine-containing, magnetic-metal-complexing beads as specific sorbents for the metal chelate affinity of albumin
    • Akgol S, Turkmen D, Denizli A: Cu(II)-incorporated, histidine-containing, magnetic-metal-complexing beads as specific sorbents for the metal chelate affinity of albumin. J Appl Polym Sci 2004, 93:2669-2677.
    • (2004) J Appl Polym Sci , vol.93 , pp. 2669-2677
    • Akgol, S.1    Turkmen, D.2    Denizli, A.3
  • 130
    • 4043086894 scopus 로고    scopus 로고
    • Porous magnetic chelator support for albumin adsorption by immobilized metal affinity separation
    • Odabasi M, Uzun L, Denizli A: Porous magnetic chelator support for albumin adsorption by immobilized metal affinity separation. J Appl Polym Sci 2004, 93:2501-2510.
    • (2004) J Appl Polym Sci , vol.93 , pp. 2501-2510
    • Odabasi, M.1    Uzun, L.2    Denizli, A.3
  • 131
    • 1442265275 scopus 로고    scopus 로고
    • Cibacron Blue F3GA-attached magnetic poly(2-hydroxyethyl methacrylate) beads for human serum albumin adsorption
    • Odabasi M, Denizli A: Cibacron Blue F3GA-attached magnetic poly(2-hydroxyethyl methacrylate) beads for human serum albumin adsorption. Polym Int 2004, 53:332-338.
    • (2004) Polym Int , vol.53 , pp. 332-338
    • Odabasi, M.1    Denizli, A.2
  • 132
    • 0034274925 scopus 로고    scopus 로고
    • Adsorption/desorption of protein on magnetic particles covered by thermosensitive polymers
    • Ding XB, Sun ZH, Zhang WC, Peng YX, Wan GX, Jiang YY: Adsorption/desorption of protein on magnetic particles covered by thermosensitive polymers. J Appl Polym Sci 2000, 77:2915-2920.
    • (2000) J Appl Polym Sci , vol.77 , pp. 2915-2920
    • Ding, X.B.1    Sun, Zh.2    Zhang, W.C.3    Peng, Y.X.4    Wan, G.X.5    Jiang, Y.Y.6
  • 133
    • 24044505136 scopus 로고    scopus 로고
    • Interactions between thermosensitive magnetic polymer microspheres and proteins
    • Ding XB, Sun ZH, Wan GX, Jiang YY: Interactions between thermosensitive magnetic polymer microspheres and proteins. Acta Polym Sinica 2000:9-13.
    • (2000) Acta Polym Sinica , pp. 9-13
    • Ding, X.B.1    Sun, Z.H.2    Wan, G.X.3    Jiang, Y.Y.4
  • 134
    • 0038025479 scopus 로고    scopus 로고
    • Preparation of highly magnetic chitosan particles and their use for affinity purification of enzymes
    • An XN, Su ZX, Zeng HM: Preparation of highly magnetic chitosan particles and their use for affinity purification of enzymes. J Chem Technol Biotechnol 2003, 78:596-560.
    • (2003) J Chem Technol Biotechnol , vol.78 , pp. 596-1560
    • An, X.N.1    Su, Z.X.2    Zeng, H.M.3
  • 135
    • 4043146513 scopus 로고    scopus 로고
    • Super-paramagnetic adsorbents for high-gradient magnetic fishing of lectins out of legume extracts
    • Heeboll-Nielsen A, Dalkiaer M, Hubbuch JJ, Thomas ORT: Super-paramagnetic adsorbents for high-gradient magnetic fishing of lectins out of legume extracts. Biotechnol Bioeng 2004, 87:311-323.
    • (2004) Biotechnol Bioeng , vol.87 , pp. 311-323
    • Heeboll-Nielsen, A.1    Dalkiaer, M.2    Hubbuch, J.J.3    Thomas, O.R.T.4
  • 136
    • 0343932797 scopus 로고    scopus 로고
    • One-step partial purification of Solanum tuberosum tuber lectin using magnetic chitosan particles
    • Safarikova M, Safarik I: One-step partial purification of Solanum tuberosum tuber lectin using magnetic chitosan particles. Biotechnol Lett 2000, 22:941-945.
    • (2000) Biotechnol Lett , vol.22 , pp. 941-945
    • Safarikova, M.1    Safarik, I.2
  • 137
    • 1642355317 scopus 로고    scopus 로고
    • Nitrilotriacetic acid-modified magnetic nanoparticles as a general agent to bind histidine-tagged proteins
    • Xu CJ, Xu KM, Gu HW, Zhong XF, Guo ZH, Zheng RK, Zhang XX, Xu B: Nitrilotriacetic acid-modified magnetic nanoparticles as a general agent to bind histidine-tagged proteins. J Am Chem Soc 2004, 126:3392-3393.
    • (2004) J Am Chem Soc , vol.126 , pp. 3392-3393
    • Xu, C.J.1    Xu, K.M.2    Gu, H.W.3    Zhong, X.F.4    Guo, Z.H.5    Zheng, R.K.6    Zhang, X.X.7    Xu, B.8
  • 138
    • 0029148183 scopus 로고
    • Novel magnetic microspheres on the basis of poly(vinyl alcohol) as affinity medium for quantitative detection of glycated hemoglobin
    • Muller-Schulte D, Brunner H: Novel magnetic microspheres on the basis of poly(vinyl alcohol) as affinity medium for quantitative detection of glycated hemoglobin. J Chromatogr A 1995, 711:53-60.
    • (1995) J Chromatogr A , vol.711 , pp. 53-60
    • Muller-Schulte, D.1    Brunner, H.2
  • 139
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • Dryden SC, Nahhas FA, Nowak JE, Goustin A-S, Tainsky MA: Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol 2003, 23:3173-3185.
    • (2003) Mol Cell Biol , vol.23 , pp. 3173-3185
    • Dryden, S.C.1    Nahhas, F.A.2    Nowak, J.E.3    Goustin, A.-S.4    Tainsky, M.A.5
  • 140
    • 0037115818 scopus 로고    scopus 로고
    • Characterization of the interaction between the nucleotide exchange factor EFTs from nematode mitochondria and elongation factor Tu
    • Ohtsuki T, Sakurai M, Sato A, Watanabe K: Characterization of the interaction between the nucleotide exchange factor EFTs from nematode mitochondria and elongation factor Tu. Nucleic Acids Res 2002, 30:5444-5451.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5444-5451
    • Ohtsuki, T.1    Sakurai, M.2    Sato, A.3    Watanabe, K.4
  • 142
    • 0025049794 scopus 로고
    • A rapid and sensitive immunoassay for tumor necrosis factor using magnetic monodisperse polymer particles
    • Liabakk NB, Nustad K, Espevik T: A rapid and sensitive immunoassay for tumor necrosis factor using magnetic monodisperse polymer particles. J Immunol Methods 1990, 134:253-259.
    • (1990) J Immunol Methods , vol.134 , pp. 253-259
    • Liabakk, N.B.1    Nustad, K.2    Espevik, T.3
  • 143
    • 0032590393 scopus 로고    scopus 로고
    • Magnetically stabilised fluidised bed adsorption: Practical benefit of uncoupling bed expansion from fluid velocities in the purification of a recombinant protein from Escherichia coli
    • Zhang ZR, O'Sullivan DA, Lyddiatt A: Magnetically stabilised fluidised bed adsorption: practical benefit of uncoupling bed expansion from fluid velocities in the purification of a recombinant protein from Escherichia coli. J Chem Technol Biotechnol 1999, 74:270-274.
    • (1999) J Chem Technol Biotechnol , vol.74 , pp. 270-274
    • Zhang, Z.R.1    O'Sullivan, D.A.2    Lyddiatt, A.3
  • 144
    • 0030907201 scopus 로고    scopus 로고
    • Sorting of MHC class II molecules and the associated invariant chain (Ii) in polarized MDCK cells
    • Simonsen A, Stang E, Bremnes B, Roe M, Prydz K, Bakke O: Sorting of MHC class II molecules and the associated invariant chain (Ii) in polarized MDCK cells. J Cell Sci 1997, 110:597-609.
    • (1997) J Cell Sci , vol.110 , pp. 597-609
    • Simonsen, A.1    Stang, E.2    Bremnes, B.3    Roe, M.4    Prydz, K.5    Bakke, O.6
  • 146
    • 0032775617 scopus 로고    scopus 로고
    • Magnetic separation to concentrate the estrogen receptor from adipose tissue for western analysis
    • Welter BH, Price TM: Magnetic separation to concentrate the estrogen receptor from adipose tissue for western analysis. Biotechniques 1999, 27:282-286.
    • (1999) Biotechniques , vol.27 , pp. 282-286
    • Welter, B.H.1    Price, T.M.2
  • 147
    • 0027505013 scopus 로고
    • Recovery of transcriptionally active chromatin restriction fragments by binding to organomercurial-agarose magnetic beads. A rapid and sensitive method for monitoring changes in higher order chromatin structure during gene activation and repression
    • Chen-Cleland TA, Boffa LC, Carpaneto EM, Mariani MR, Valentin E, Mendez E, Allfrey VG: Recovery of transcriptionally active chromatin restriction fragments by binding to organomercurial-agarose magnetic beads. A rapid and sensitive method for monitoring changes in higher order chromatin structure during gene activation and repression. J Biol Chem 1993, 268:23409-23416.
    • (1993) J Biol Chem , vol.268 , pp. 23409-23416
    • Chen-Cleland, T.A.1    Boffa, L.C.2    Carpaneto, E.M.3    Mariani, M.R.4    Valentin, E.5    Mendez, E.6    Allfrey, V.G.7
  • 148
    • 0028791344 scopus 로고
    • Insulin resistance is mediated by a proteolytic fragment of the insulin receptor
    • Knutson VP, Donnelly PV, Balba Y, Lopez-Reyes M: Insulin resistance is mediated by a proteolytic fragment of the insulin receptor. J Biol Chem 1995, 270:24972-24981.
    • (1995) J Biol Chem , vol.270 , pp. 24972-24981
    • Knutson, V.P.1    Donnelly, P.V.2    Balba, Y.3    Lopez-Reyes, M.4
  • 149
    • 0032915401 scopus 로고    scopus 로고
    • Identification of a novel Stat3 recruitment and activation motif within the granulocyte colony-stimulating factor receptor
    • Chakraborty A, Dyer KF, Cascio M, Mietzner TA, Tweardy DJ: Identification of a novel Stat3 recruitment and activation motif within the granulocyte colony-stimulating factor receptor. Blood 1999, 93:15-24.
    • (1999) Blood , vol.93 , pp. 15-24
    • Chakraborty, A.1    Dyer, K.F.2    Cascio, M.3    Mietzner, T.A.4    Tweardy, D.J.5
  • 150
    • 0034782173 scopus 로고    scopus 로고
    • Detection of HbA(1c) by boronate affinity immunoassay using bacterial magnetic particles
    • Tanaka T, Matsunaga T: Detection of HbA(1c) by boronate affinity immunoassay using bacterial magnetic particles. Biosens Bioelectron 2001, 16:1089-1094.
    • (2001) Biosens Bioelectron , vol.16 , pp. 1089-1094
    • Tanaka, T.1    Matsunaga, T.2
  • 151
    • 0026410275 scopus 로고
    • Analysis and isolation of human transferrin receptor using the OKT-9 monoclonal antibody covalently cross-linked to magnetic beads
    • Karlsson GB, Platt FM: Analysis and isolation of human transferrin receptor using the OKT-9 monoclonal antibody covalently cross-linked to magnetic beads. Anal Biochem 1991, 199:219-222.
    • (1991) Anal Biochem , vol.199 , pp. 219-222
    • Karlsson, G.B.1    Platt, F.M.2
  • 152
    • 0035853471 scopus 로고    scopus 로고
    • Analysis of proteins in the extracellular matrix of the plant pathogenic fungus Bipolaris sorokiniana using 2-D gel electrophoresis and MS/MS
    • Apoga D, Ek B, Tunlid A: Analysis of proteins in the extracellular matrix of the plant pathogenic fungus Bipolaris sorokiniana using 2-D gel electrophoresis and MS/MS. FEMS Microbiol Lett 2001, 197:145-150.
    • (2001) FEMS Microbiol Lett , vol.197 , pp. 145-150
    • Apoga, D.1    Ek, B.2    Tunlid, A.3
  • 154
    • 0033566997 scopus 로고    scopus 로고
    • Purification of prostate-specific antigen from human serum by indirect immunosorption and elution with a hapten
    • Peter J, Unverzagt C, Lenz H, Hoesel W: Purification of prostate-specific antigen from human serum by indirect immunosorption and elution with a hapten. Anal Biochem 1999, 273:98-104.
    • (1999) Anal Biochem , vol.273 , pp. 98-104
    • Peter, J.1    Unverzagt, C.2    Lenz, H.3    Hoesel, W.4
  • 155
    • 0035113880 scopus 로고    scopus 로고
    • Identification of precursor forms of free prostate-specific antigen in serum of prostate cancer patients by immunosorption and mass spectrometry
    • Peter J, Unverzagt C, Krogh TN, Vorm O, Hoesel W: Identification of precursor forms of free prostate-specific antigen in serum of prostate cancer patients by immunosorption and mass spectrometry. Cancer Res 2001, 61:957-962.
    • (2001) Cancer Res , vol.61 , pp. 957-962
    • Peter, J.1    Unverzagt, C.2    Krogh, T.N.3    Vorm, O.4    Hoesel, W.5
  • 156
    • 0035146301 scopus 로고    scopus 로고
    • BR22, a novel protein, interacts with thyroid transcription factor-1 and activates the human surfactant protein B promoter
    • Yang Y-S, Yang M-CW, Wang B, Weissler JC: BR22, a novel protein, interacts with thyroid transcription factor-1 and activates the human surfactant protein B promoter. Am J Respir Cell Mol Biol 2001, 24:30-37.
    • (2001) Am J Respir Cell Mol Biol , vol.24 , pp. 30-37
    • Yang, Y.-S.1    Yang, M.-C.W.2    Wang, B.3    Weissler, J.C.4
  • 157
    • 0348196654 scopus 로고    scopus 로고
    • Efficient isolation, purification, and characterization of the Helicoverpa zea VHDL receptor
    • Persaud DR, Yousefi V, Haunerland N: Efficient isolation, purification, and characterization of the Helicoverpa zea VHDL receptor. Protein Expr Purif 2003, 32:260-264.
    • (2003) Protein Expr Purif , vol.32 , pp. 260-264
    • Persaud, D.R.1    Yousefi, V.2    Haunerland, N.3
  • 158
    • 0034445784 scopus 로고    scopus 로고
    • Purification and characterization of a 200 kDa fructosyllysine-specific binding protein from cell membranes of U937 cells
    • Salazar R, Brandt R, Kellermann J, Krantz S: Purification and characterization of a 200 kDa fructosyllysine-specific binding protein from cell membranes of U937 cells. Glycoconjugate J 2000, 17:713-716.
    • (2000) Glycoconjugate J , vol.17 , pp. 713-716
    • Salazar, R.1    Brandt, R.2    Kellermann, J.3    Krantz, S.4
  • 159
    • 0030200912 scopus 로고    scopus 로고
    • Coupling of MALDI-TOF mass analysis to the separation of biotinylated peptides by magnetic streptavidin beads
    • Girault S, Chassaing G, Blais JC, Brunot A, Bolbach G: Coupling of MALDI-TOF mass analysis to the separation of biotinylated peptides by magnetic streptavidin beads. Anal Chem 1996, 68:2122-2126.
    • (1996) Anal Chem , vol.68 , pp. 2122-2126
    • Girault, S.1    Chassaing, G.2    Blais, J.C.3    Brunot, A.4    Bolbach, G.5
  • 160
    • 0030571021 scopus 로고    scopus 로고
    • Development of magnetic beads for rapid and efficient metal-chelate affinity purifications
    • Ji Z, Pinon DI, Miller LJ: Development of magnetic beads for rapid and efficient metal-chelate affinity purifications. Anal Biochem 1996, 240:197-201.
    • (1996) Anal Biochem , vol.240 , pp. 197-201
    • Ji, Z.1    Pinon, D.I.2    Miller, L.J.3
  • 161
    • 15444348069 scopus 로고
    • Screening of a synthetic pentapeptide library composed of D-amino acids against fructose-1,6-biphosphate aldolase
    • Samson I, Rozenski J, Vanaerschot A, Samyn B, Vanbeeumen J, Herdewijn P: Screening of a synthetic pentapeptide library composed of D-amino acids against fructose-1,6-biphosphate aldolase. Lett Pept Sci 1995, 2:259-260.
    • (1995) Lett Pept Sci , vol.2 , pp. 259-260
    • Samson, I.1    Rozenski, J.2    Vanaerschot, A.3    Samyn, B.4    Vanbeeumen, J.5    Herdewijn, P.6
  • 163
    • 0034489620 scopus 로고    scopus 로고
    • Rapid purification of nisin Z using specific monoclonal antibody-coated magnetic beads
    • Prioult G, Turcotte C, Labarre L, Lacroix C, Fliss I: Rapid purification of nisin Z using specific monoclonal antibody-coated magnetic beads. Int Dairy J 2000, 10:627-633.
    • (2000) Int Dairy J , vol.10 , pp. 627-633
    • Prioult, G.1    Turcotte, C.2    Labarre, L.3    Lacroix, C.4    Fliss, I.5


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