메뉴 건너뛰기




Volumn 13, Issue 5, 2004, Pages 1379-1390

Direct measurement of protein osmotic second virial cross coefficients by cross-interaction chromatography

Author keywords

chymotrypsinogen; BSA; Lysozyme; Membrane osmometry; Protein interactions; Protein separations; Self association; Static light scattering

Indexed keywords

BOVINE SERUM ALBUMIN; LYSOZYME;

EID: 1942473133     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03419204     Document Type: Article
Times cited : (62)

References (39)
  • 1
    • 0033009529 scopus 로고    scopus 로고
    • Analysis of the thermodynamic non-ideality of proteins by sedimentation equilibrium experiments
    • Behlke, J. and Ristau, O. 1999. Analysis of the thermodynamic non-ideality of proteins by sedimentation equilibrium experiments. Biophys. Chem. 76: 13-23.
    • (1999) Biophys. Chem. , vol.76 , pp. 13-23
    • Behlke, J.1    Ristau, O.2
  • 2
    • 0030811146 scopus 로고    scopus 로고
    • Different tools to study interaction potentials in γ-crystallin solutions: Relevance to crystal growth
    • Bonneté, F., Malfois, M., Finet, S., Tardieu, A., Lafont, S., and Veesler, S. 1997. Different tools to study interaction potentials in γ-crystallin solutions: Relevance to crystal growth. Acta Crystallogr. D 53: 438-447.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 438-447
    • Bonneté, F.1    Malfois, M.2    Finet, S.3    Tardieu, A.4    Lafont, S.5    Veesler, S.6
  • 3
    • 0018359663 scopus 로고
    • Determination of the molecular weight of proteins in heterogeneous mixtures: Use of an air-driven ultra-centrifuge for the analysis of protein-protein interactions
    • Clarke, R.G. and Howlett, G.J. 1979. Determination of the molecular weight of proteins in heterogeneous mixtures: Use of an air-driven ultra-centrifuge for the analysis of protein-protein interactions. Arch. Biochem. Biophys. 195: 235-242.
    • (1979) Arch. Biochem. Biophys. , vol.195 , pp. 235-242
    • Clarke, R.G.1    Howlett, G.J.2
  • 4
    • 0032484699 scopus 로고    scopus 로고
    • Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes
    • Curtis, R.A., Prausnitz, J.M., and Blanch, H.W. 1998. Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes. Biotechnol. Bioeng. 57: 11-21.
    • (1998) Biotechnol. Bioeng. , vol.57 , pp. 11-21
    • Curtis, R.A.1    Prausnitz, J.M.2    Blanch, H.W.3
  • 5
    • 0037143801 scopus 로고    scopus 로고
    • Protein-protein interactions in concentrated electrolyte solutions: Hofmeister-series effects
    • Curtis, R.A., Ulrich, J., Montaser, A., Prausnitz, J.M., and Blanch, H.W. 2002. Protein-protein interactions in concentrated electrolyte solutions: Hofmeister-series effects. Biotechnol. Bioeng. 79: 367-380.
    • (2002) Biotechnol. Bioeng. , vol.79 , pp. 367-380
    • Curtis, R.A.1    Ulrich, J.2    Montaser, A.3    Prausnitz, J.M.4    Blanch, H.W.5
  • 6
    • 0034705635 scopus 로고    scopus 로고
    • Pore size distributions of cation-exchange adsorbents determined by inverse size-exclusion chromatography
    • DePhillips, P. and Lenhoff, A.M. 2000. Pore size distributions of cation-exchange adsorbents determined by inverse size-exclusion chromatography. J. Chromatogr. A 883: 39-54.
    • (2000) J. Chromatogr. A , vol.883 , pp. 39-54
    • DePhillips, P.1    Lenhoff, A.M.2
  • 7
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • George, A. and Wilson, W.W. 1994. Predicting protein crystallization from a dilute solution property. Acta Crystallogr. D 50: 361-365.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 8
    • 0015218725 scopus 로고
    • Interacting systems of type a + b reversible c: Ovalbumin and myoglobin
    • Gilbert, G.A. and Kellett, G.L. 1971. Interacting systems of type a + b reversible c: Ovalbumin and myoglobin. J. Biol. Chem. 246: 6079-6086.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6079-6086
    • Gilbert, G.A.1    Kellett, G.L.2
  • 9
    • 0001578536 scopus 로고
    • Thermodynamic properties of aqueous α-chymotrypsin solutions from membrane osmometry measurements
    • Haynes, C.A., Tamura, K., Korfer, H.R., Blanch, H.W., and Prausnitz, J.M. 1992. Thermodynamic properties of aqueous α-chymotrypsin solutions from membrane osmometry measurements. J. Phys. Chem. 96: 905-912.
    • (1992) J. Phys. Chem. , vol.96 , pp. 905-912
    • Haynes, C.A.1    Tamura, K.2    Korfer, H.R.3    Blanch, H.W.4    Prausnitz, J.M.5
  • 12
    • 84988119892 scopus 로고
    • Studies on the electrostatic interactions of lysozyme with α-lactalbumin and β-lactoglobulin
    • Howell, N.K., Yeboah, N.A., and Lewis, D.F.V. 1995. Studies on the electrostatic interactions of lysozyme with α-lactalbumin and β-lactoglobulin. Int. J. Food Sci. Tech. 30: 813-824.
    • (1995) Int. J. Food Sci. Tech. , vol.30 , pp. 813-824
    • Howell, N.K.1    Yeboah, N.A.2    Lewis, D.F.V.3
  • 13
    • 0015935119 scopus 로고
    • Sedimentation equilibrium study of interaction between ovalbumin and lysozyme
    • Howlett, G.J. and Nichol, L.W. 1973. Sedimentation equilibrium study of interaction between ovalbumin and lysozyme. J. Biol. Chem. 248: 619-621.
    • (1973) J. Biol. Chem. , vol.248 , pp. 619-621
    • Howlett, G.J.1    Nichol, L.W.2
  • 16
    • 0023441919 scopus 로고
    • Osmotic pressure measurements of ovalbumin and lysozyme mixtures
    • McCarty, B.W. and Adams, E.T. 1987. Osmotic pressure measurements of ovalbumin and lysozyme mixtures. Biophys. Chem. 28: 149-159.
    • (1987) Biophys. Chem. , vol.28 , pp. 149-159
    • McCarty, B.W.1    Adams, E.T.2
  • 18
    • 0034349193 scopus 로고    scopus 로고
    • Protein-protein interactions in aqueous ammonium sulfate solutions: Lysozyme and bovine serum albumin (BSA)
    • Moon, Y.U., Curtis, R.A., Anderson, C.O., Blanch, H.W., and Prausnitz, J.M. 2000. Protein-protein interactions in aqueous ammonium sulfate solutions: Lysozyme and bovine serum albumin (BSA). J. Solution Chem. 29: 699-717.
    • (2000) J. Solution Chem. , vol.29 , pp. 699-717
    • Moon, Y.U.1    Curtis, R.A.2    Anderson, C.O.3    Blanch, H.W.4    Prausnitz, J.M.5
  • 19
    • 0029289456 scopus 로고
    • Excluded volume contribution to the osmotic second virial coefficient for proteins
    • Neal, B.L. and Lenhoff, A.M. 1995. Excluded volume contribution to the osmotic second virial coefficient for proteins. AIChE J. 41: 1010-1014.
    • (1995) AIChE J. , vol.41 , pp. 1010-1014
    • Neal, B.L.1    Lenhoff, A.M.2
  • 20
    • 0031723926 scopus 로고    scopus 로고
    • Molecular origins of osmotic second virial coefficients of proteins
    • Neal, B.L., Asthagiri, D., and Lenhoff, A.M. 1998. Molecular origins of osmotic second virial coefficients of proteins. Biophys. J. 75: 2469-2477.
    • (1998) Biophys. J. , vol.75 , pp. 2469-2477
    • Neal, B.L.1    Asthagiri, D.2    Lenhoff, A.M.3
  • 21
    • 0001746158 scopus 로고
    • Determination of equilibrium constants from transport data on rapidly reacting systems of type a plus b to from c
    • Nichol, L.W. and Winzor, D.J. 1964. Determination of equilibrium constants from transport data on rapidly reacting systems of type a plus b to from c. J. Phys. Chem. 68: 2455-2463.
    • (1964) J. Phys. Chem. , vol.68 , pp. 2455-2463
    • Nichol, L.W.1    Winzor, D.J.2
  • 22
    • 0014122288 scopus 로고
    • Evaluation of gel filtration data on systems interacting chemically and physically
    • Nichol, L.W., Ogston, A.G., and Winzor, D.J. 1967. Evaluation of gel filtration data on systems interacting chemically and physically. Arch. Biochem. Biophys. 121: 517-521.
    • (1967) Arch. Biochem. Biophys. , vol.121 , pp. 517-521
    • Nichol, L.W.1    Ogston, A.G.2    Winzor, D.J.3
  • 23
    • 0018068655 scopus 로고
    • Study of multiple polymerization equilibria by glass bead exclusion chromatography with allowance for thermodynamic non-ideality effects
    • Nichol, L.W., Siezen, R.J., and Winzor, D.J. 1978. Study of multiple polymerization equilibria by glass bead exclusion chromatography with allowance for thermodynamic non-ideality effects. Biophys. Chem. 9: 47-55.
    • (1978) Biophys. Chem. , vol.9 , pp. 47-55
    • Nichol, L.W.1    Siezen, R.J.2    Winzor, D.J.3
  • 24
    • 0002445915 scopus 로고
    • Structure of adsorbed and desorbed proteins
    • Norde, W. and Favier, J.P. 1992. Structure of adsorbed and desorbed proteins. Colloid. Suface. 64: 87-93.
    • (1992) Colloid. Suface , vol.64 , pp. 87-93
    • Norde, W.1    Favier, J.P.2
  • 25
    • 10144225635 scopus 로고    scopus 로고
    • Self-interaction chromatography: A tool for the study of protein-protein interactions in bioprocessing environments
    • Patro, S.Y. and Przybycien, T.M. 1996. Self-interaction chromatography: A tool for the study of protein-protein interactions in bioprocessing environments. Biotechnol. Bioeng. 52: 193-203.
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 193-203
    • Patro, S.Y.1    Przybycien, T.M.2
  • 26
    • 52449146817 scopus 로고
    • Immobilization of binding proteins on nonporous supports: Comparison of protein loading, activity, and stability
    • Plant, A.L., Locascio-Brown, L., Haller, W., and Durst, R.A. 1991. Immobilization of binding proteins on nonporous supports: Comparison of protein loading, activity, and stability. Appl. Biochem. Biotech. 30: 83-98.
    • (1991) Appl. Biochem. Biotech. , vol.30 , pp. 83-98
    • Plant, A.L.1    Locascio-Brown, L.2    Haller, W.3    Durst, R.A.4
  • 27
    • 0008624908 scopus 로고
    • Determination of virial coefficients of protein solutions by means of X-ray small-angle scattering and interpretations
    • Porschel, H.V., and Damaschun, G. 1977. Determination of virial coefficients of protein solutions by means of X-ray small-angle scattering and interpretations. Stud. Biophys. 62: 69.
    • (1977) Stud. Biophys. , vol.62 , pp. 69
    • Porschel, H.V.1    Damaschun, G.2
  • 28
    • 1942489414 scopus 로고    scopus 로고
    • High thoughput tools for the development of physically stabilized protein formulations
    • Paper presented, Boston
    • Przybycien, T.M. and Wilcox, A. 2002. High thoughput tools for the development of physically stabilized protein formulations. Paper presented at ACS National Meeting, Boston.
    • (2002) ACS National Meeting
    • Przybycien, T.M.1    Wilcox, A.2
  • 29
    • 0030606890 scopus 로고    scopus 로고
    • Study of protein binding to a silica support with a polymeric cation-exchange coating
    • Ratnayake, C.K. and Regnier, F.E. 1996. Study of protein binding to a silica support with a polymeric cation-exchange coating. J. Chromatogr. A 743: 15-23.
    • (1996) J. Chromatogr. A , vol.743 , pp. 15-23
    • Ratnayake, C.K.1    Regnier, F.E.2
  • 30
    • 0024969402 scopus 로고
    • Relative effectiveness of various ions on the solubility and crystal growth of lysozyme
    • Ries-Kautt, M.M. and Ducruix, A.F. 1989. Relative effectiveness of various ions on the solubility and crystal growth of lysozyme. J. Biol. Chem. 264: 745-748.
    • (1989) J. Biol. Chem. , vol.264 , pp. 745-748
    • Ries-Kautt, M.M.1    Ducruix, A.F.2
  • 31
    • 0030566439 scopus 로고    scopus 로고
    • Protein interactions and crystallization
    • Rosenbaum, D.F. and Zukoski, C.F. 1996. Protein interactions and crystallization. J. Cryst. Growth 169: 752-758.
    • (1996) J. Cryst. Growth , vol.169 , pp. 752-758
    • Rosenbaum, D.F.1    Zukoski, C.F.2
  • 32
    • 1842268670 scopus 로고
    • Reversible association processes of globular proteins, 2: Electrostatic complexes of plasma albumin and lysozyme
    • Steiner, R.F. 1953a. Reversible association processes of globular proteins, 2: Electrostatic complexes of plasma albumin and lysozyme. Arch. Biochem. Biophys. 47: 56-75.
    • (1953) Arch. Biochem. Biophys. , vol.47 , pp. 56-75
    • Steiner, R.F.1
  • 33
    • 1942456969 scopus 로고
    • Reversible association processes of globular proteins, 4: Fluorescence methods in studying protein interactions
    • -. 1953b. Reversible association processes of globular proteins, 4: Fluorescence methods in studying protein interactions. Arch. Biochem. Biophys. 46: 291-311.
    • (1953) Arch. Biochem. Biophys. , vol.46 , pp. 291-311
  • 34
    • 0036194842 scopus 로고    scopus 로고
    • Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography
    • Tessier, P.M., Lenhoff, A.M., and Sandler, S.I. 2002a. Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography. Biophys. J. 82: 1620-1631.
    • (2002) Biophys. J. , vol.82 , pp. 1620-1631
    • Tessier, P.M.1    Lenhoff, A.M.2    Sandler, S.I.3
  • 36
    • 1942489413 scopus 로고    scopus 로고
    • Correlation of diafiltration sieving behavior of lysozyme-BSA mixtures with osmotic second virial cross coefficients
    • in press
    • Tessier, P.M., Verruto, V.J., Sandler, S.I., and Lenhoff, A.M. 2004. Correlation of diafiltration sieving behavior of lysozyme-BSA mixtures with osmotic second virial cross coefficients. Biotechnol. Bioeng. (in press).
    • (2004) Biotechnol. Bioeng.
    • Tessier, P.M.1    Verruto, V.J.2    Sandler, S.I.3    Lenhoff, A.M.4
  • 37
    • 0031768735 scopus 로고    scopus 로고
    • Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen
    • Velev, O.D., Kaler, E.W., and Lenhoff, A.M. 1998. Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen. Biophys. J. 75: 2682-2697.
    • (1998) Biophys. J. , vol.75 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 38
    • 49049146776 scopus 로고
    • The osmotic pressure of concentrated protein solutions: Effect of concentration and pH in saline solutions of bovine serum albumin
    • Vilker, V.L., Colton, C.K., and Smith, K.A. 1981. The osmotic pressure of concentrated protein solutions: Effect of concentration and pH in saline solutions of bovine serum albumin. J. Colloid Interface Sci. 79: 548-566.
    • (1981) J. Colloid Interface Sci. , vol.79 , pp. 548-566
    • Vilker, V.L.1    Colton, C.K.2    Smith, K.A.3
  • 39
    • 36849131807 scopus 로고
    • Applications of the methods of molecular distribution to solutions of large molecules
    • Zimm, B.H. 1946. Applications of the methods of molecular distribution to solutions of large molecules. J. Chem. Phys. 14: 164-179.
    • (1946) J. Chem. Phys. , vol.14 , pp. 164-179
    • Zimm, B.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.