메뉴 건너뛰기




Volumn 25, Issue 2, 1996, Pages 85-129

Recent developments in the use of group-specific ligands for affinity bioseparations

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; BIOTECHNOLOGY; CHEMICAL ACTIVATION; CHEMICAL BONDS; COST EFFECTIVENESS; ENZYME IMMOBILIZATION; EXTRACTION; FLUOROCARBONS; MEMBRANES; MICELLES; PRECIPITATION (CHEMICAL); ULTRAFILTRATION;

EID: 0030366097     PISSN: 03602540     EISSN: None     Source Type: Journal    
DOI: 10.1080/03602549608001293     Document Type: Article
Times cited : (7)

References (107)
  • 2
    • 0038108919 scopus 로고
    • Novel separation based on affinity interactions
    • Luong, J. H. T., and Nguyen, A.-L., 1992. Novel separation based on affinity interactions. Adv. Biochem. Eng., 47: 137
    • (1992) Adv. Biochem. Eng. , vol.47 , pp. 137
    • Luong, J.H.T.1    Nguyen, A.-L.2
  • 4
    • 0015328664 scopus 로고
    • Some studies on insolubilized nicotinamide nucleotide
    • Dean, P. D. G., and Lowe, C. R., 1972. Some studies on insolubilized nicotinamide nucleotide. Biochem. J., 127: 11P
    • (1972) Biochem. J. , vol.127 , pp. 11P
    • Dean, P.D.G.1    Lowe, C.R.2
  • 5
    • 0015518628 scopus 로고
    • Some applications of insolubilized cofactors to the purification of pyridine nucleotide-dependent dehydrogenases
    • Lowe, C. R., Mosbach, K., and Dean, P. D. G., 1972. Some applications of insolubilized cofactors to the purification of pyridine nucleotide-dependent dehydrogenases. Biochem. Biophys. Res. Commun., 48: 1004
    • (1972) Biochem. Biophys. Res. Commun. , vol.48 , pp. 1004
    • Lowe, C.R.1    Mosbach, K.2    Dean, P.D.G.3
  • 6
    • 0016220917 scopus 로고
    • AMP and NAD as ‘general ligands’
    • Mosbach, K., 1974. AMP and NAD as ‘general ligands’. Methods Enzymol., 34: 229
    • (1974) Methods Enzymol. , vol.34 , pp. 229
    • Mosbach, K.1
  • 7
    • 0020011459 scopus 로고
    • Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by Streptococci and Pneumonococci
    • Langone, J. J., 1982. Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by Streptococci and Pneumonococci. Adv. Immunol., 32: 157
    • (1982) Adv. Immunol. , vol.32 , pp. 157
    • Langone, J.J.1
  • 8
    • 24644492624 scopus 로고
    • Introduction to the use of reactive dyes in biotechnology
    • Clonis Y.D., Atkinson T., Bruton C.J., Lowe C.R., (eds), New York: Stockton Press,. Edited by
    • Lowe, C. R., 1987. “ Introduction to the use of reactive dyes in biotechnology ”. In Reactive Dyes in Protein and Enzyme Technology, Edited by: Clonis, Y. D., Atkinson, T., Bruton, C. J., and Lowe, C. R., 1New York: Stockton Press.
    • (1987) Reactive Dyes in Protein and Enzyme Technology , pp. 1
    • Lowe, C.R.1
  • 9
    • 0026470134 scopus 로고
    • Purification of biologically active human plasma transthyretin by dye-affinity chromatography: Studies on dye leakage and possibility of heat treatment for virus inactivation
    • Regnault, V., Rivat, C., Vallar, L., Geschier, C., and Stoltz, J. F., 1992. Purification of biologically active human plasma transthyretin by dye-affinity chromatography: Studies on dye leakage and possibility of heat treatment for virus inactivation. J. Chromatogr., 584: 93
    • (1992) J. Chromatogr. , vol.584 , pp. 93
    • Regnault, V.1    Rivat, C.2    Vallar, L.3    Geschier, C.4    Stoltz, J.F.5
  • 13
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography: A new approach to protein fractionation
    • Porath, J., Carlsson, J., Olsson, I., and Belfrage, G., 1975. Metal chelate affinity chromatography: A new approach to protein fractionation. Nature, 258: 598
    • (1975) Nature , vol.258 , pp. 598
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 14
    • 0026071781 scopus 로고
    • Metal-affinity separations: A new dimension in protein processing
    • Arnold, F. H., 1991. Metal-affinity separations: A new dimension in protein processing. Bio/Technology, 9: 151
    • (1991) Bio/Technology , vol.9 , pp. 151
    • Arnold, F.H.1
  • 15
    • 0001760837 scopus 로고
    • Hard and soft acids and bases
    • Pearson, R. G., 1967. Hard and soft acids and bases. Chem. Br., 3: 103
    • (1967) Chem. Br. , vol.3 , pp. 103
    • Pearson, R.G.1
  • 16
    • 0010827721 scopus 로고
    • Hard and soft acids and bases, HSAB, Part I, Fundamental principles
    • Pearson, R. G., 1968. Hard and soft acids and bases, HSAB, Part I, Fundamental principles. J. Chem. Educ, 45: 581
    • (1968) J. Chem. Educ , vol.45 , pp. 581
    • Pearson, R.G.1
  • 17
    • 33749034799 scopus 로고
    • Hard and soft acids and bases, HSAB, Part II, Underlying Theories
    • Pearson, R. G., 1968. Hard and soft acids and bases, HSAB, Part II, Underlying Theories. J. Chem. Educ, 45: 643
    • (1968) J. Chem. Educ , vol.45 , pp. 643
    • Pearson, R.G.1
  • 18
    • 0028796529 scopus 로고
    • Retention behavior of amino acids using immobilized Ag(I) chromatography
    • Kim, D.-H., and García, A. A., 1995. Retention behavior of amino acids using immobilized Ag(I) chromatography. Biotechnol. Prog., 11
    • (1995) Biotechnol. Prog. , vol.11
    • Kim, D.-H.1    García, A.A.2
  • 19
    • 77957004737 scopus 로고
    • Protein fractionation on the basis of solubility in aqueous solution of salts and organic solvents
    • Green, A. A., and Hughes, W. L., 1955. Protein fractionation on the basis of solubility in aqueous solution of salts and organic solvents. Methods Enzymol., 1: 67
    • (1955) Methods Enzymol. , vol.1 , pp. 67
    • Green, A.A.1    Hughes, W.L.2
  • 21
    • 0002423852 scopus 로고
    • Affinity precipitation
    • Street G., (ed), London: Blackie Academic and Professional, and,. Edited by
    • Gupta, M. N., and Mattiasson, B., 1994. “ Affinity precipitation ”. In Highly Selective Separations in Biotechnology, Edited by: Street, G., 7London: Blackie Academic and Professional.
    • (1994) Highly Selective Separations in Biotechnology , pp. 7
    • Gupta, M.N.1    Mattiasson, B.2
  • 23
    • 0009463974 scopus 로고
    • Precipitation
    • Asenjo J.A., (ed), New York: Marcel Dekker,. Edited by
    • Glatz, C. E., 1990. “ Precipitation ”. In Separation Processes in Biotechnology 2, Edited by: Asenjo, J. A., 329New York: Marcel Dekker.
    • (1990) Separation Processes in Biotechnology 2 , pp. 329
    • Glatz, C.E.1
  • 24
    • 0018790602 scopus 로고
    • Affinity precipitation of enzymes
    • Larsson, P.-O., and Mosbach, K., 1979. Affinity precipitation of enzymes. FEBS Lett., 98: 333
    • (1979) FEBS Lett. , vol.98 , pp. 333
    • Larsson, P.-O.1    Mosbach, K.2
  • 26
    • 84911755348 scopus 로고
    • Dye-ligand affinity precipitation
    • Clonis Y.D., Atkinson T., Bruton C.J., Lowe C.R., (eds), New York: Stockton Press,. Edited by
    • Pearson, J. C., 1987. “ Dye-ligand affinity precipitation ”. In Reactive Dyes in Protein and Enzyme Technology, Edited by: Clonis, Y. D., Atkinson, T., Bruton, C. J., and Lowe, C. R., 187New York: Stockton Press.
    • (1987) Reactive Dyes in Protein and Enzyme Technology , pp. 187
    • Pearson, J.C.1
  • 27
    • 0023006886 scopus 로고
    • Affinity precipitation of lactate dehydrogenase with a triazine dye derivative: Selective precipitation of rabbit muscle lactate dehydrogenase with a Procion Blue H-B analog
    • Pearson, J. C., Burton, S. J., and Lowe, C. R., 1986. Affinity precipitation of lactate dehydrogenase with a triazine dye derivative: Selective precipitation of rabbit muscle lactate dehydrogenase with a Procion Blue H-B analog. Anal Biochem., 158: 382
    • (1986) Anal Biochem. , vol.158 , pp. 382
    • Pearson, J.C.1    Burton, S.J.2    Lowe, C.R.3
  • 28
    • 0025701085 scopus 로고
    • Complications encountered using Cibacron Blue F3G-A as a ligand for affinity precipitation of lactate dehydrogenase
    • Morris, J. E., and Fisher, R. R., 1990. Complications encountered using Cibacron Blue F3G-A as a ligand for affinity precipitation of lactate dehydrogenase. Biotech. Bioeng., 36: 737
    • (1990) Biotech. Bioeng. , vol.36 , pp. 737
    • Morris, J.E.1    Fisher, R.R.2
  • 30
    • 0024306539 scopus 로고
    • Evaluation of the interaction of peptides with Cu(II), Ni(II), and Zn(II) by high-performance immobilized metal ion affinity chromatography
    • Yip, T.-T., Nakagawa, Y., and Porath, J., 1989. Evaluation of the interaction of peptides with Cu(II), Ni(II), and Zn(II) by high-performance immobilized metal ion affinity chromatography. Anal. Biochem., 183: 159
    • (1989) Anal. Biochem. , vol.183 , pp. 159
    • Yip, T.-T.1    Nakagawa, Y.2    Porath, J.3
  • 31
    • 0000844197 scopus 로고
    • Surface topography of histidine residues: A facile probe by immobilized metal ion affinity chromatography
    • Hedman, E. S., Zhao, Y., Sulkowski, E., and Porath, J., 1989. Surface topography of histidine residues: A facile probe by immobilized metal ion affinity chromatography. Proc. Nat. Acad. Sci., USA, 86: 1811
    • (1989) Proc. Nat. Acad. Sci., USA , vol.86 , pp. 1811
    • Hedman, E.S.1    Zhao, Y.2    Sulkowski, E.3    Porath, J.4
  • 32
    • 0028052836 scopus 로고
    • Copper affinity precipitation as an initial step in protein purification
    • Agarwal, R., and Gupta, M. N., 1994. Copper affinity precipitation as an initial step in protein purification. Biotech. Tech., 8: 655
    • (1994) Biotech. Tech. , vol.8 , pp. 655
    • Agarwal, R.1    Gupta, M.N.2
  • 33
    • 0000092386 scopus 로고
    • Immobilized iminodiacetic acid metal peptide complexes. Identification of a chelating peptide purification handles for recombinant proteins
    • Smith, M. C., Furan, T. C., and Pidgeon, C., 1987. Immobilized iminodiacetic acid metal peptide complexes. Identification of a chelating peptide purification handles for recombinant proteins. Inorg. Chem., 26: 1965
    • (1987) Inorg. Chem. , vol.26 , pp. 1965
    • Smith, M.C.1    Furan, T.C.2    Pidgeon, C.3
  • 35
    • 0005027409 scopus 로고
    • Affinity precipitation
    • Ngo T.T., (ed), New York: Plenum Press, and,. Edited by
    • Mattiasson, B., and Kaul, R., 1993. “ Affinity precipitation ”. In Molecular Interactions in Bioseparations, Edited by: Ngo, T. T., 469New York: Plenum Press.
    • (1993) Molecular Interactions in Bioseparations , pp. 469
    • Mattiasson, B.1    Kaul, R.2
  • 36
    • 84988057766 scopus 로고
    • Affinity-precipitation using chitosan as a ligand carrier
    • Senstad, C., and Mattiasson, B., 1989. Affinity-precipitation using chitosan as a ligand carrier. Biotech. Bioeng., 33: 216
    • (1989) Biotech. Bioeng. , vol.33 , pp. 216
    • Senstad, C.1    Mattiasson, B.2
  • 37
    • 0027551965 scopus 로고
    • Production of cellobiose by enzymatic hydrolysis: Removal of β-glucosidase from cellulase by affinity precipitation using chitosan
    • Homma, T., Fujii, M., Mori, J.-I., Kawakami, T., Kuroda, K., and Taniguchi, M., 1993. Production of cellobiose by enzymatic hydrolysis: Removal of β-glucosidase from cellulase by affinity precipitation using chitosan. Biotech. Bioeng., 41: 405
    • (1993) Biotech. Bioeng. , vol.41 , pp. 405
    • Homma, T.1    Fujii, M.2    Mori, J.-I.3    Kawakami, T.4    Kuroda, K.5    Taniguchi, M.6
  • 38
    • 0028294566 scopus 로고
    • Purification of the D-lactate dehydrogenase from Leuconostoc-mesenteroides ssp Cremoris using a sequential precipitation procedure
    • Shu, H. C., Dong, C. Q., Kaul, R., and Mattiasson, B., 1994. Purification of the D-lactate dehydrogenase from Leuconostoc-mesenteroides ssp Cremoris using a sequential precipitation procedure. J. Biotech., 34: 1
    • (1994) J. Biotech. , vol.34 , pp. 1
    • Shu, H.C.1    Dong, C.Q.2    Kaul, R.3    Mattiasson, B.4
  • 39
    • 0028357985 scopus 로고
    • Integration of aqueous two-phase extraction and affinity precipitation for the purification of lactate dehydrogenase
    • Guoqiang, D., Kaul, R., and Mattiasson, B., 1994. Integration of aqueous two-phase extraction and affinity precipitation for the purification of lactate dehydrogenase. J. Chrom. A, 668: 145
    • (1994) J. Chrom. A , vol.668 , pp. 145
    • Guoqiang, D.1    Kaul, R.2    Mattiasson, B.3
  • 40
    • 0025391442 scopus 로고
    • Alginate as immobilization matrix for cells
    • Smidsrød, O., and Skjak-Braek, G., 1990. Alginate as immobilization matrix for cells. Trends Biotech., 8: 71
    • (1990) Trends Biotech. , vol.8 , pp. 71
    • Smidsrød, O.1    Skjak-Braek, G.2
  • 41
    • 0001978348 scopus 로고
    • Evaluation of alginate as a ligand carrier in affinity precipitation
    • Linné, E., Garg, N., Kaul, R., and Mattiasson, B., 1992. Evaluation of alginate as a ligand carrier in affinity precipitation. Biotech. Appl. Biochem., 16: 48
    • (1992) Biotech. Appl. Biochem. , vol.16 , pp. 48
    • Linné, E.1    Garg, N.2    Kaul, R.3    Mattiasson, B.4
  • 42
    • 0028539339 scopus 로고
    • Temperature responsive bioconjugates. 3. Antibody-poly(N-isopropylacrylamide) conjugates for temperature-modulated precipitations and affinity bioseparations
    • Takei, Y. G., Matsukata, M., Aoki, T., Sanui, K., Ogata, N., Kikuchi, A., Sakurai, Y., and Okano, T., 1994. Temperature responsive bioconjugates. 3. Antibody-poly(N-isopropylacrylamide) conjugates for temperature-modulated precipitations and affinity bioseparations. Bioconj. Chem., 5: 577
    • (1994) Bioconj. Chem. , vol.5 , pp. 577
    • Takei, Y.G.1    Matsukata, M.2    Aoki, T.3    Sanui, K.4    Ogata, N.5    Kikuchi, A.6    Sakurai, Y.7    Okano, T.8
  • 43
    • 0028406270 scopus 로고
    • Purification of rabbit C-reactive protein by affinity precipitation with thermosensitive polymer
    • Mori, S., Nakata, Y., and Endo, H., 1994. Purification of rabbit C-reactive protein by affinity precipitation with thermosensitive polymer. Prot. Expres. Purif., 5: 153
    • (1994) Prot. Expres. Purif. , vol.5 , pp. 153
    • Mori, S.1    Nakata, Y.2    Endo, H.3
  • 44
    • 0028501262 scopus 로고
    • Affinity thermoprecipitation of lactate-dehydrogenase and pyruvate-kinase from porcine muscle using Eudragit bound Cibacron Blue
    • Guoqiang, D., Lali, A., Kaul, R., and Mattiasson, B., 1994. Affinity thermoprecipitation of lactate-dehydrogenase and pyruvate-kinase from porcine muscle using Eudragit bound Cibacron Blue. J. Biotech., 37: 23
    • (1994) J. Biotech. , vol.37 , pp. 23
    • Guoqiang, D.1    Lali, A.2    Kaul, R.3    Mattiasson, B.4
  • 45
    • 0027604973 scopus 로고
    • Affinity thermoprecipitation: Contribution of the efficiency of ligand-protein interaction and access of the ligand
    • Galaev, I. Y., and Mattiasson, B., 1993. Affinity thermoprecipitation: Contribution of the efficiency of ligand-protein interaction and access of the ligand. Biotech. Bioeng., 41: 1101
    • (1993) Biotech. Bioeng. , vol.41 , pp. 1101
    • Galaev, I.Y.1    Mattiasson, B.2
  • 47
    • 0026918461 scopus 로고
    • Affinity precipitation of proteins by surfactant-solubiiized, ligand-modified phospholipids
    • Powers, D. D., Willard, B. L., Carbonell, R. G., and Kilpatrick, P. K., 1992. Affinity precipitation of proteins by surfactant-solubiiized, ligand-modified phospholipids. Biotechnol. Prog., 8: 436
    • (1992) Biotechnol. Prog. , vol.8 , pp. 436
    • Powers, D.D.1    Willard, B.L.2    Carbonell, R.G.3    Kilpatrick, P.K.4
  • 48
    • 0026597301 scopus 로고
    • Surface-modified membranes as a matrix for protein purification
    • Langlotz, P., and Kroner, K. H., 1992. Surface-modified membranes as a matrix for protein purification. J. Chromatogr., 591: 107
    • (1992) J. Chromatogr. , vol.591 , pp. 107
    • Langlotz, P.1    Kroner, K.H.2
  • 49
    • 0026643577 scopus 로고
    • Studies of a novel membrane for affinity separations. I. Functionalisation and protein coupling
    • Bamford, C. H., Al-Lamee, K. G., Purbrick, M. D., and Wear, T. J., 1992. Studies of a novel membrane for affinity separations. I. Functionalisation and protein coupling. J. Chromatogr., 606: 19
    • (1992) J. Chromatogr. , vol.606 , pp. 19
    • Bamford, C.H.1    Al-Lamee, K.G.2    Purbrick, M.D.3    Wear, T.J.4
  • 50
    • 0028519528 scopus 로고
    • Chitosan modified sulfonated poly (ethersulfone) as a support for affinity separations
    • Klein, E., Eichholz, E., Theimer, F., and Yeager, D., 1994. Chitosan modified sulfonated poly (ethersulfone) as a support for affinity separations. J. Membr. Sci., 95: 199
    • (1994) J. Membr. Sci. , vol.95 , pp. 199
    • Klein, E.1    Eichholz, E.2    Theimer, F.3    Yeager, D.4
  • 51
    • 0025052246 scopus 로고
    • Novel affinity-based processes for protein purification
    • Chen, J.-P., 1990. Novel affinity-based processes for protein purification. J. Ferment. Bioeng., 70: 199
    • (1990) J. Ferment. Bioeng. , vol.70 , pp. 199
    • Chen, J.-P.1
  • 52
    • 2142786199 scopus 로고
    • Membrane-based affinity separation processes
    • Street G., (ed), London: Blackie Academic and Professional,. Edited by
    • Malakian, A., 1994. “ Membrane-based affinity separation processes ”. In Highly Selective Separations in Biotechnology, Edited by: Street, G., 34London: Blackie Academic and Professional.
    • (1994) Highly Selective Separations in Biotechnology , pp. 34
    • Malakian, A.1
  • 53
    • 0000067944 scopus 로고
    • Modification of microfiltration membranes as dye-ligand adsorbents for the isolation of enzymes from crude extractants
    • Pyle D.L., (ed), London: Elsevier, and,. Edited by
    • Champluvier, B., and Kula, M.-R., 1990. “ Modification of microfiltration membranes as dye-ligand adsorbents for the isolation of enzymes from crude extractants ”. In Separations for Biotechnology 2, Edited by: Pyle, D. L., 295London: Elsevier.
    • (1990) Separations for Biotechnology 2 , pp. 295
    • Champluvier, B.1    Kula, M.-R.2
  • 54
    • 0003393340 scopus 로고
    • Dye-grafted poly (ethylene imine)-coated, formed-in-place class affinity membrane for selective separation of proteins
    • Shalaby S.W., Ikada Y., Langer R., Williams J., (eds), Washington, D. C.: American Chemical Society, and,. Edited by
    • Li, Y., and Spencer, H. G., 1994. “ Dye-grafted poly (ethylene imine)-coated, formed-in-place class affinity membrane for selective separation of proteins ”. In Polymers of Biological and Biomedical Significance, Edited by: Shalaby, S. W, Ikada, Y., Langer, R., and Williams, J., 297Washington, D. C.: American Chemical Society.
    • (1994) Polymers of Biological and Biomedical Significance , pp. 297
    • Li, Y.1    Spencer, H.G.2
  • 56
    • 0028096887 scopus 로고
    • Membrane affinity chromatography of alkaline phosphatase
    • Guo, W., Shang, Z., Yu, Y., and Zhou, L., 1994. Membrane affinity chromatography of alkaline phosphatase. J. Chromatogr. A, 685: 344
    • (1994) J. Chromatogr. A , vol.685 , pp. 344
    • Guo, W.1    Shang, Z.2    Yu, Y.3    Zhou, L.4
  • 57
    • 0028389056 scopus 로고
    • Synthesis and characterization of affinity membranes made from polysulfone
    • Rodemann, K., and Staude, E., 1994. Synthesis and characterization of affinity membranes made from polysulfone. J. Membr. Sci., 88: 271
    • (1994) J. Membr. Sci. , vol.88 , pp. 271
    • Rodemann, K.1    Staude, E.2
  • 58
    • 0028764674 scopus 로고
    • Protein fractionation using fast flow immobilized metal chelate affinity membrane
    • Serafica, G. C., Pimbley, J., and Belford, G., 1994. Protein fractionation using fast flow immobilized metal chelate affinity membrane. Biotechnol. Bioeng., 43: 21
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 21
    • Serafica, G.C.1    Pimbley, J.2    Belford, G.3
  • 59
    • 0024278495 scopus 로고
    • Synthesis and characterization of a water-soluble affinity polymer for trypsin purification
    • Luong, J. H. T., Male, K. B., and Nguyen, A. L., 1988. Synthesis and characterization of a water-soluble affinity polymer for trypsin purification. Biotechnol. Bioeng., 31: 439
    • (1988) Biotechnol. Bioeng. , vol.31 , pp. 439
    • Luong, J.H.T.1    Male, K.B.2    Nguyen, A.L.3
  • 60
    • 0023996776 scopus 로고
    • A continuous affinity ultrafiltration process for trypsin purification
    • Luong, J. H. T., Male, K. B., and Nguyen, A. L., 1988. A continuous affinity ultrafiltration process for trypsin purification. Biotechnol. Bioeng., 31: 516
    • (1988) Biotechnol. Bioeng. , vol.31 , pp. 516
    • Luong, J.H.T.1    Male, K.B.2    Nguyen, A.L.3
  • 61
    • 0025700084 scopus 로고
    • Isolation of urokinase by affinity ultrafiltration
    • Male, K. B., Nguyen, A. L., and Luong, J. H. T., 1990. Isolation of urokinase by affinity ultrafiltration. Biotechnol. Bioeng., 35: 87
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 87
    • Male, K.B.1    Nguyen, A.L.2    Luong, J.H.T.3
  • 62
    • 0342712725 scopus 로고
    • Macroligand D-alanyl-D-alanine-dextran Vancomycin purification. Equilibrium binding study
    • Lee, C. K., Pan, L. C., and Ju, Y. H., 1994. Macroligand D-alanyl-D-alanine-dextran Vancomycin purification. Equilibrium binding study. Appl. Biochem. Biotechnol., 44: 21
    • (1994) Appl. Biochem. Biotechnol. , vol.44 , pp. 21
    • Lee, C.K.1    Pan, L.C.2    Ju, Y.H.3
  • 64
    • 84911760883 scopus 로고
    • Aqueous two-phase affinity partitioning
    • Clonis Y.D., Atkinson T., Bruton C.J., Lowe C.R., (eds), New York: Stockton Press,. Edited by
    • Johanson, G., 1987. “ Aqueous two-phase affinity partitioning ”. In Reactive Dyes in Protein and Enzyme Technology, Edited by: Clonis, Y. D, Atkinson, T., Bruton, C. J., and Lowe, C. R., 101New York: Stockton Press.
    • (1987) Reactive Dyes in Protein and Enzyme Technology , pp. 101
    • Johanson, G.1
  • 65
    • 0024038172 scopus 로고
    • Factors influencing the use of aqueous two-phase partition for protein purification
    • Carlson, A., 1988. Factors influencing the use of aqueous two-phase partition for protein purification. Sep. Sci. Technol, 23: 785
    • (1988) Sep. Sci. Technol , vol.23 , pp. 785
    • Carlson, A.1
  • 66
    • 0025405524 scopus 로고
    • A mathematical model for metal affinity protein partitioning
    • Suh, S.-S., and Arnold, F. H., 1990. A mathematical model for metal affinity protein partitioning. Biotechnol. Bioeng., 35: 682
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 682
    • Suh, S.-S.1    Arnold, F.H.2
  • 67
    • 0027013383 scopus 로고
    • Aqueous two-phase systems for biomolecule separation
    • Diamond, A. D., and Hsu, J. T., 1992. Aqueous two-phase systems for biomolecule separation. Adv. Biochem. Eng., 47: 89
    • (1992) Adv. Biochem. Eng. , vol.47 , pp. 89
    • Diamond, A.D.1    Hsu, J.T.2
  • 68
    • 0023667361 scopus 로고
    • Affinity partitioning of enzymes using dextran-bound Procion Yellow HE-3G. Influence of dye-ligand density
    • Johansson, G., and Joelsson, M., 1987. Affinity partitioning of enzymes using dextran-bound Procion Yellow HE-3G. Influence of dye-ligand density. J. Chromatog., 393: 195
    • (1987) J. Chromatog. , vol.393 , pp. 195
    • Johansson, G.1    Joelsson, M.2
  • 69
    • 0028277481 scopus 로고
    • Partitioning of blood proteins using immobilized dyes
    • Birkenmeier, G., 1994. Partitioning of blood proteins using immobilized dyes. Methods Enzymol., 228: 154
    • (1994) Methods Enzymol. , vol.228 , pp. 154
    • Birkenmeier, G.1
  • 70
    • 0025668472 scopus 로고
    • Combination of polymer-bound charged groups and affinity ligands for extraction of enzymes by partitioning in aqueous two-phase systems
    • Cheng, L., Joelsson, M., and Johansson, G., 1990. Combination of polymer-bound charged groups and affinity ligands for extraction of enzymes by partitioning in aqueous two-phase systems. J. Chromatog., 523: 119
    • (1990) J. Chromatog. , vol.523 , pp. 119
    • Cheng, L.1    Joelsson, M.2    Johansson, G.3
  • 71
    • 0028337620 scopus 로고
    • Purification of lactate dehydrogenase from pig muscle by affinity partitioning
    • Joelsson, M., and Tjerneld, F., 1994. Purification of lactate dehydrogenase from pig muscle by affinity partitioning. Methods Enzymol., 228: 136
    • (1994) Methods Enzymol. , vol.228 , pp. 136
    • Joelsson, M.1    Tjerneld, F.2
  • 72
    • 0028357985 scopus 로고
    • Integration of aqueous two-phase extraction and affinity precipitation for the purification of lactate dehydrogenase
    • Guoqiang, D., Kaul, R., and Mattiasson, B., 1994. Integration of aqueous two-phase extraction and affinity precipitation for the purification of lactate dehydrogenase. J. Chromatog. A, 668: 145
    • (1994) J. Chromatog. A , vol.668 , pp. 145
    • Guoqiang, D.1    Kaul, R.2    Mattiasson, B.3
  • 73
    • 0028338251 scopus 로고
    • Phosphofructokinase from baker's yeast
    • Koppschläger, G., 1994. Phosphofructokinase from baker's yeast. Methods Enzymol, 228: 144
    • (1994) Methods Enzymol , vol.228 , pp. 144
    • Koppschläger, G.1
  • 74
    • 0000699730 scopus 로고
    • Aqueous two-phase metal affinity extraction of heme proteins
    • Wuenschell, G. E., Naranjo, E., and Arnold, F. H., 1990. Aqueous two-phase metal affinity extraction of heme proteins. Bioproc. Eng., 5: 199
    • (1990) Bioproc. Eng. , vol.5 , pp. 199
    • Wuenschell, G.E.1    Naranjo, E.2    Arnold, F.H.3
  • 76
    • 0027027515 scopus 로고
    • Enzyme purification by immobilized metal ion affinity partitioning. Application of D-hydroxyisocaproate dehydrogenase
    • Schustolla, D., Deckwer, W. D., Schugerl, K., and Hustedt, H., 1992. Enzyme purification by immobilized metal ion affinity partitioning. Application of D-hydroxyisocaproate dehydrogenase. Bioseparation, 3: 167
    • (1992) Bioseparation , vol.3 , pp. 167
    • Schustolla, D.1    Deckwer, W.D.2    Schugerl, K.3    Hustedt, H.4
  • 77
    • 0027257163 scopus 로고
    • Recognition and separation of isoenzymes by metal chelates. Immobilized metal ion affinity partitioning of lactate dehydrogenase isoenzymes
    • Otto, A., and Birkenmeier, G., 1993. Recognition and separation of isoenzymes by metal chelates. Immobilized metal ion affinity partitioning of lactate dehydrogenase isoenzymes. J. Chromatog., 644: 25
    • (1993) J. Chromatog. , vol.644 , pp. 25
    • Otto, A.1    Birkenmeier, G.2
  • 79
    • 0004186246 scopus 로고
    • The use of reverse miscelles for the separation of proteins
    • Street G., (ed), London: Blackie Academic and Professional, and,. Edited by
    • Dekker, M., and Leser, M. E., 1994. “ The use of reverse miscelles for the separation of proteins ”. In Highly Selective Separations in Biotechnology, Edited by: Street, G., 86London: Blackie Academic and Professional.
    • (1994) Highly Selective Separations in Biotechnology , pp. 86
    • Dekker, M.1    Leser, M.E.2
  • 80
    • 9444221725 scopus 로고
    • Reverse micelles for protein purification
    • Ngo T.T., (ed), New York: Plenum Press,. Edited by
    • Dekker, M., 1993. “ Reverse micelles for protein purification ”. In Molecular Interactions in Bioseparations, Edited by: Ngo, T. T., 533New York: Plenum Press.
    • (1993) Molecular Interactions in Bioseparations , pp. 533
    • Dekker, M.1
  • 81
    • 0001875306 scopus 로고
    • Bioaffinity separations using reversed micellar extraction
    • Woll, J. M., Hatton, T. A., and Yarmush, M. L., 1989. Bioaffinity separations using reversed micellar extraction. Biotechnol. Prog., 5: 57
    • (1989) Biotechnol. Prog. , vol.5 , pp. 57
    • Woll, J.M.1    Hatton, T.A.2    Yarmush, M.L.3
  • 82
    • 0026191837 scopus 로고
    • Purification of glycoproteins by selective transport using concanavalin-mediated reverse micellar extraction
    • Paradkar, V. M., and Dordick, J. S., 1991. Purification of glycoproteins by selective transport using concanavalin-mediated reverse micellar extraction. Biotechnol. Prog., 7: 330
    • (1991) Biotechnol. Prog. , vol.7 , pp. 330
    • Paradkar, V.M.1    Dordick, J.S.2
  • 83
    • 0028446945 scopus 로고
    • Extraction of concanavalin A with affinity reversed micellar system
    • Chen, J.-P., and Jen, J.-T., 1994. Extraction of concanavalin A with affinity reversed micellar system. Sep. Sci. Technol., 29: 1115
    • (1994) Sep. Sci. Technol. , vol.29 , pp. 1115
    • Chen, J.-P.1    Jen, J.-T.2
  • 84
    • 0027703728 scopus 로고
    • Affinity-based reversed micellar protein extraction: II. Effect of cosurfactant tail length
    • Kelley, B. D., Wang, D. I. C., and Hatton, T. A., 1993. Affinity-based reversed micellar protein extraction: II. Effect of cosurfactant tail length. Biotechnol. Bioeng., 42: 1209
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 1209
    • Kelley, B.D.1    Wang, D.I.C.2    Hatton, T.A.3
  • 85
    • 0027551859 scopus 로고
    • Reverse micelles in protein separation: The use of silica for the back-transfer process
    • Leser, M. E., Mrkoci, K., and Luisi, P. L., 1993. Reverse micelles in protein separation: The use of silica for the back-transfer process. Biotechnol. Bioeng., 41: 489
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 489
    • Leser, M.E.1    Mrkoci, K.2    Luisi, P.L.3
  • 86
    • 0027703828 scopus 로고
    • Affinity-based reversed micellar protein extraction: I. Principles and protein-ligand system
    • Kelley, B. D., Wang, D. I. C., and Hatton, T. A., 1993. Affinity-based reversed micellar protein extraction: I. Principles and protein-ligand system. Biotechnol. Bioeng., 42: 1199
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 1199
    • Kelley, B.D.1    Wang, D.I.C.2    Hatton, T.A.3
  • 87
    • 0024713875 scopus 로고
    • Affinity chromatography of triazine dyes immobilised on novel perfluorocarbon supports
    • Steward, D. J., Hughes, P., and Lowe, C. R., 1989. Affinity chromatography of triazine dyes immobilised on novel perfluorocarbon supports. J. Biotechnol., 11: 253
    • (1989) J. Biotechnol. , vol.11 , pp. 253
    • Steward, D.J.1    Hughes, P.2    Lowe, C.R.3
  • 88
    • 0024734232 scopus 로고
    • Affinity separations using liquid perfluorocarbon supports: Rate effects
    • Broedeker, A. R., and Lenhoff, A. M., 1989. Affinity separations using liquid perfluorocarbon supports: Rate effects. Biotechnol. Prog., 5: 132
    • (1989) Biotechnol. Prog. , vol.5 , pp. 132
    • Broedeker, A.R.1    Lenhoff, A.M.2
  • 89
    • 0026563275 scopus 로고
    • Novel affinity separations based on perfluorocarbon emulsions. Use of a perfluorocarbon affinity emulsion for the purification of human serum albumin from blood plasma in a fluidised bed
    • McCreath, G. E., Chase, H. A., Purvis, D. R., and Lowe, C. R., 1992. Novel affinity separations based on perfluorocarbon emulsions. Use of a perfluorocarbon affinity emulsion for the purification of human serum albumin from blood plasma in a fluidised bed. J. Chromatogr., 597: 189
    • (1992) J. Chromatogr. , vol.597 , pp. 189
    • McCreath, G.E.1    Chase, H.A.2    Purvis, D.R.3    Lowe, C.R.4
  • 90
    • 0027397833 scopus 로고
    • Novel affinity separations based on perfluorocarbon emulsions. Development of a perfluorocarbon emulsion reactor for continuous affinity separations and its application in the purification of human serum albumin from blood plasma
    • McCreath, G. E., Chase, H. A., Purvis, D. R., and Lowe, C. R., 1993. Novel affinity separations based on perfluorocarbon emulsions. Development of a perfluorocarbon emulsion reactor for continuous affinity separations and its application in the purification of human serum albumin from blood plasma. J. Chromatogr., 629: 201
    • (1993) J. Chromatogr. , vol.629 , pp. 201
    • McCreath, G.E.1    Chase, H.A.2    Purvis, D.R.3    Lowe, C.R.4
  • 91
    • 0028044876 scopus 로고
    • Novel affinity separations based on perfluorocarbon emulsions. Use of a perfluorocarbon affinity emulsion for the direct extraction of glucose-6-phosphate dehydrogenase from homogenised baker's yeast
    • McCreath, G. E., Chase, H. A., and Lowe, C. R., 1994. Novel affinity separations based on perfluorocarbon emulsions. Use of a perfluorocarbon affinity emulsion for the direct extraction of glucose-6-phosphate dehydrogenase from homogenised baker's yeast. J. Chromatogr., 659: 275
    • (1994) J. Chromatogr. , vol.659 , pp. 275
    • McCreath, G.E.1    Chase, H.A.2    Lowe, C.R.3
  • 92
    • 0027435888 scopus 로고
    • Protein purification by dye-ligand chromatography
    • Boyer, P. M., and Hsu, J. T., 1993. Protein purification by dye-ligand chromatography. Adv. Biochem. Eng., 49: 1
    • (1993) Adv. Biochem. Eng. , vol.49 , pp. 1
    • Boyer, P.M.1    Hsu, J.T.2
  • 93
    • 0026391951 scopus 로고
    • Immobilized metal ion affinity chromatography (IMAC) - Chemistry and bioseparation applications
    • Wong, J. W., Albright, R. L., and Wang, N.-H. L., 1991. Immobilized metal ion affinity chromatography (IMAC) - Chemistry and bioseparation applications. Sep. Purif. Methods., 20: 49
    • (1991) Sep. Purif. Methods. , vol.20 , pp. 49
    • Wong, J.W.1    Albright, R.L.2    Wang, N.H.L.3
  • 94
    • 0027248458 scopus 로고
    • behaviour of polyhydroxyethyl methacrylate sorbent with dextran-filled macropores in dye-affinity chromatography of proteins
    • Mislovicová, D., Petro, M., and Berek, D., 1993. behaviour of polyhydroxyethyl methacrylate sorbent with dextran-filled macropores in dye-affinity chromatography of proteins. J. Chromatogr., 646: 411
    • (1993) J. Chromatogr. , vol.646 , pp. 411
    • Mislovicová, D.1    Petro, M.2    Berek, D.3
  • 95
    • 0027957763 scopus 로고
    • Poly(N-vinylpyrrolidone) shielding of matrices for dye-affinity chromatography. Improved elution of lactate dehydrogenase from Blue Sepharose and secondary alcohol dehydrogenase from Scarlet Sepharose
    • Galaev, I. Y., and Mattiason, B., 1994. Poly(N-vinylpyrrolidone) shielding of matrices for dye-affinity chromatography. Improved elution of lactate dehydrogenase from Blue Sepharose and secondary alcohol dehydrogenase from Scarlet Sepharose. J. Chromatogr. A, 662: 27
    • (1994) J. Chromatogr. A , vol.662 , pp. 27
    • Galaev, I.Y.1    Mattiason, B.2
  • 96
    • 0028151288 scopus 로고
    • Interaction of Cibacron Blue with polymers: Implications for polymer-shielded dye-affinity chromatography of phosphofructokinase from baker's yeast
    • Galaev, I. Y., Garg, N., and Mattiason, B., 1994. Interaction of Cibacron Blue with polymers: implications for polymer-shielded dye-affinity chromatography of phosphofructokinase from baker's yeast. J. Chromatogr. A, 684: 45
    • (1994) J. Chromatogr. A , vol.684 , pp. 45
    • Galaev, I.Y.1    Garg, N.2    Mattiason, B.3
  • 97
    • 0028276259 scopus 로고
    • Studies of the interaction of NADH oxidase from Thermus thermophilus HB8 with triazine dyes
    • Kirchberger, J., Erdmann, H., Hecht, H.-J., and Kopperschläger, G., 1994. Studies of the interaction of NADH oxidase from Thermus thermophilus HB8 with triazine dyes. J. Chromatogr. A, 668: 153
    • (1994) J. Chromatogr. A , vol.668 , pp. 153
    • Kirchberger, J.1    Erdmann, H.2    Hecht, H.-J.3    Kopperschläger, G.4
  • 98
    • 0028231173 scopus 로고
    • Chromatography of human immunoglobulin G on immobilized Drimarene Rubine R/K-5BL. Study of mild, efficient elution procedures
    • Cochet, S., Hasnaoui, M., Debbia, M., Kroviarski, Y., Lambin, P., Cartron, J. P., and Bertrand, O., 1994. Chromatography of human immunoglobulin G on immobilized Drimarene Rubine R/K-5BL. Study of mild, efficient elution procedures. J. Chromatogr. A, 663: 175
    • (1994) J. Chromatogr. A , vol.663 , pp. 175
    • Cochet, S.1    Hasnaoui, M.2    Debbia, M.3    Kroviarski, Y.4    Lambin, P.5    Cartron, J.P.6    Bertrand, O.7
  • 99
    • 0026447573 scopus 로고
    • Purification of S-oxynitrilase from Sorghum bicolor by immobilized metal ion affinity chromatography on different carrier materials
    • Woker, R., Champluvier, B., and Kula, M.-R., 1992. Purification of S-oxynitrilase from Sorghum bicolor by immobilized metal ion affinity chromatography on different carrier materials. J. Chromatogr. B, 584: 85
    • (1992) J. Chromatogr. B , vol.584 , pp. 85
    • Woker, R.1    Champluvier, B.2    Kula, M.-R.3
  • 100
    • 0028157408 scopus 로고
    • Multiple-site binding interactions in metal-affinity chromatography. I. Equilibrium binding of engineered histidine-containing cytochromes c
    • Todd, R. J., Johnson, R. D., and Arnold, F. H., 1994. Multiple-site binding interactions in metal-affinity chromatography. I. Equilibrium binding of engineered histidine-containing cytochromes c. J. Chromatogr. A, 662: 13
    • (1994) J. Chromatogr. A , vol.662 , pp. 13
    • Todd, R.J.1    Johnson, R.D.2    Arnold, F.H.3
  • 101
    • 0027092610 scopus 로고
    • Immobilized metal ion affinity chromatography of synthetic peptides. Binding via the α-amino group
    • Hansen, P., Lindeberg, G., and Andersson, L., 1992. Immobilized metal ion affinity chromatography of synthetic peptides. Binding via the α-amino group. J. Chromatogr., 627: 125
    • (1992) J. Chromatogr. , vol.627 , pp. 125
    • Hansen, P.1    Lindeberg, G.2    Andersson, L.3
  • 102
    • 0028978254 scopus 로고
    • Importance of the α-amino group in the selective purification of synthetic histidine peptides by immobilised metal ion affinity chromatography
    • Hansen, P., and Lindeberg, G., 1995. Importance of the α-amino group in the selective purification of synthetic histidine peptides by immobilised metal ion affinity chromatography. J. Chromatogr. A, 690: 155
    • (1995) J. Chromatogr. A , vol.690 , pp. 155
    • Hansen, P.1    Lindeberg, G.2
  • 103
    • 0028935311 scopus 로고
    • Rapid one-step purification of goat immunoglobulins by immobilized metal ion affinity chromatography
    • Boden, V., Winzerling, J. J., Vijayalakshmi, M., and Porath, J., 1995. Rapid one-step purification of goat immunoglobulins by immobilized metal ion affinity chromatography. J. Immunol. Meth., 181: 225
    • (1995) J. Immunol. Meth. , vol.181 , pp. 225
    • Boden, V.1    Winzerling, J.J.2    Vijayalakshmi, M.3    Porath, J.4
  • 104
    • 0028764978 scopus 로고
    • Purification of a recombinant protein produced in a baculovirus expression system by immobilized metal affinity chromatography
    • Wang, M.-Y., Bentley, W. E., and Vakharia, V., 1994. Purification of a recombinant protein produced in a baculovirus expression system by immobilized metal affinity chromatography. Biotechnol. Bioeng., 43: 349
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 349
    • Wang, M.-Y.1    Bentley, W.E.2    Vakharia, V.3
  • 105
    • 0028524562 scopus 로고
    • Immobilized of silver and platinum ions for metal affinity chromatography
    • García, A. A., Kim, D. H., and Miles, D. R., 1994. Immobilized of silver and platinum ions for metal affinity chromatography. Reactive Polymers, 23: 249
    • (1994) Reactive Polymers , vol.23 , pp. 249
    • García, A.A.1    Kim, D.H.2    Miles, D.R.3
  • 106
    • 0029035918 scopus 로고
    • Separation of biotin labeled proteins from their unlabeled counterparts using immobilized platinum affinity chromatography
    • Miles, D. R., and García, A. A., 1995. Separation of biotin labeled proteins from their unlabeled counterparts using immobilized platinum affinity chromatography. J. Chromatogr. A, 702: 173
    • (1995) J. Chromatogr. A , vol.702 , pp. 173
    • Miles, D.R.1    García, A.A.2
  • 107
    • 0028860046 scopus 로고
    • Membrane chromatography - An integrative concept in the downstream processing of proteins
    • Thömmes, J., and Kula, M.-R., 1995. Membrane chromatography - An integrative concept in the downstream processing of proteins. Biotechnol. Prog., 11: 357
    • (1995) Biotechnol. Prog. , vol.11 , pp. 357
    • Thömmes, J.1    Kula, M.-R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.