메뉴 건너뛰기




Volumn 53, Issue 2, 2011, Pages 216-222

Self-interaction chromatography of proteins on a microfluidic monolith

Author keywords

Catalase; Chromatographic monolith; Osmotic second virial coefficient; Protein solution thermodynamics; Protein protein interactions

Indexed keywords

CATALASE; CHROMATOGRAPHIC MONOLITH; PROTEIN SOLUTION THERMODYNAMICS; PROTEIN-PROTEIN INTERACTIONS; SECOND VIRIAL COEFFICIENTS;

EID: 78649917900     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2010.10.016     Document Type: Article
Times cited : (13)

References (51)
  • 1
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • George A., Wilson W.W. Predicting protein crystallization from a dilute solution property. Acta Crystallogr. D: Biol. Crystallogr. 1994, 50:361-365.
    • (1994) Acta Crystallogr. D: Biol. Crystallogr. , vol.50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 3
    • 33748290394 scopus 로고    scopus 로고
    • Screening for physical stability of a Pseudomonas amylase using self-interaction chromatography
    • Valente J.J., Fryksdale B.G., Dale D.A., Gaertner A.L., Henry C.S. Screening for physical stability of a Pseudomonas amylase using self-interaction chromatography. Anal. Biochem. 2006, 357:35-42.
    • (2006) Anal. Biochem. , vol.357 , pp. 35-42
    • Valente, J.J.1    Fryksdale, B.G.2    Dale, D.A.3    Gaertner, A.L.4    Henry, C.S.5
  • 4
    • 33845965334 scopus 로고    scopus 로고
    • Ultrasonic storage modulus as a novel parameter for analyzing protein-protein interactions in high protein concentration solution: correlation with static and dynamic light scattering measurements
    • Saluja A., Badkar A.V., Zeng D.L., Nema S., Kalonia D.S. Ultrasonic storage modulus as a novel parameter for analyzing protein-protein interactions in high protein concentration solution: correlation with static and dynamic light scattering measurements. Biophys. J. 2007, 92:234-244.
    • (2007) Biophys. J. , vol.92 , pp. 234-244
    • Saluja, A.1    Badkar, A.V.2    Zeng, D.L.3    Nema, S.4    Kalonia, D.S.5
  • 5
    • 38349042010 scopus 로고    scopus 로고
    • Protein phase behavior in aqueous solutions: crystallization, liquid-liquid phase separation, gels and aggregate
    • Dumetz A.C., Chockla A.M., Kaler E.W., Lenhoff A.M. Protein phase behavior in aqueous solutions: crystallization, liquid-liquid phase separation, gels and aggregate. Biophys. J. 2008, 94:570-583.
    • (2008) Biophys. J. , vol.94 , pp. 570-583
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 6
    • 0000566578 scopus 로고
    • Light scattering in solutions of serum albumin: effects of charge and ionic strength
    • Edsall J.T., Edelhoch H., Lontie R., Morrison P.R. Light scattering in solutions of serum albumin: effects of charge and ionic strength. J. Am. Chem. Soc. 1950, 72:4641-4656.
    • (1950) J. Am. Chem. Soc. , vol.72 , pp. 4641-4656
    • Edsall, J.T.1    Edelhoch, H.2    Lontie, R.3    Morrison, P.R.4
  • 8
    • 0029278478 scopus 로고
    • Salting out of aqueous proteins-phase equilibria and intermolecular potentials
    • Coen C.J., Blanch H.W., Prausnitz J.M. Salting out of aqueous proteins-phase equilibria and intermolecular potentials. AIChE J. 1995, 41:996-1004.
    • (1995) AIChE J. , vol.41 , pp. 996-1004
    • Coen, C.J.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 9
    • 0029540627 scopus 로고
    • Interactions in undersaturated and supersaturated lysozyme solutions: static and dynamic light scattering results
    • Muschol M., Rosenberger F. Interactions in undersaturated and supersaturated lysozyme solutions: static and dynamic light scattering results. J. Chem. Phys. 1995, 103:10424-10432.
    • (1995) J. Chem. Phys. , vol.103 , pp. 10424-10432
    • Muschol, M.1    Rosenberger, F.2
  • 10
    • 0030566439 scopus 로고    scopus 로고
    • Protein interactions and crystallization
    • Rosenbaum D.F., Zukoski C.F. Protein interactions and crystallization. J. Cryst. Growth 1996, 169:752-758.
    • (1996) J. Cryst. Growth , vol.169 , pp. 752-758
    • Rosenbaum, D.F.1    Zukoski, C.F.2
  • 11
    • 17844405882 scopus 로고    scopus 로고
    • A consistent experimental and modeling approach to light scattering studies of protein-protein interactions in solution
    • Asthagiri D., Paliwal A., Abras D., Lenhoff A.M., Paulaitis M.E. A consistent experimental and modeling approach to light scattering studies of protein-protein interactions in solution. Biophys. J. 2005, 88:3300-3309.
    • (2005) Biophys. J. , vol.88 , pp. 3300-3309
    • Asthagiri, D.1    Paliwal, A.2    Abras, D.3    Lenhoff, A.M.4    Paulaitis, M.E.5
  • 12
    • 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., Lenhoff A.M. Protein interactions in solution characterized by light and neutron scattering: comparison of lysozyme and chymotrypsinogen. Biophys. J. 1998, 75:2682-2697.
    • (1998) Biophys. J. , vol.75 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 13
    • 0001578536 scopus 로고
    • Thermodynamic properties of aqueous α-chymotrypsin solutions from membrane osmometry
    • Haynes C.A., Tamura K., Korfer H.R., Blanch H.W., Prausnitz J.M. Thermodynamic properties of aqueous α-chymotrypsin solutions from membrane osmometry. J. Phys. Chem. 1992, 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
  • 14
    • 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., Smith K.A. The osmotic pressure of concentrated protein solutions: effect of concentration and pH in saline solutions of bovine serum albumin. J. Colloids Interface Sci. 1981, 79:548-566.
    • (1981) J. Colloids Interface Sci. , vol.79 , pp. 548-566
    • Vilker, V.L.1    Colton, C.K.2    Smith, K.A.3
  • 15
    • 0030565979 scopus 로고    scopus 로고
    • Protein interactions as seen by solution X-ray scattering prior to crystallogenesis
    • Ducruix A., Guilloteau J.P., Ries-Kautt M., Tardieu A. Protein interactions as seen by solution X-ray scattering prior to crystallogenesis. J. Cryst. Growth 1996, 168:28-39.
    • (1996) J. Cryst. Growth , vol.168 , pp. 28-39
    • Ducruix, A.1    Guilloteau, J.P.2    Ries-Kautt, M.3    Tardieu, A.4
  • 16
    • 0031954146 scopus 로고    scopus 로고
    • Lysozyme crystal growth, as observed by small angle X-ray scattering, proceeds without crystallization intermediates
    • Finet S., Bonnete F., Frouin J., Provost K., Tardieu A. Lysozyme crystal growth, as observed by small angle X-ray scattering, proceeds without crystallization intermediates. Eur. Biophys. J. Biophys. Lett. 1998, 27:263-271.
    • (1998) Eur. Biophys. J. Biophys. Lett. , vol.27 , pp. 263-271
    • Finet, S.1    Bonnete, F.2    Frouin, J.3    Provost, K.4    Tardieu, A.5
  • 18
    • 0036006284 scopus 로고    scopus 로고
    • X-ray scattering studies of Aspergillus flavus urate oxidase: towards a better understanding of PEG effects on the crystallization of large proteins
    • Vivares D., Bonnete F. X-ray scattering studies of Aspergillus flavus urate oxidase: towards a better understanding of PEG effects on the crystallization of large proteins. Acta Crystallogr. D: Biol. Crystallogr. 2002, 58:472-479.
    • (2002) Acta Crystallogr. D: Biol. Crystallogr. , vol.58 , pp. 472-479
    • Vivares, D.1    Bonnete, F.2
  • 19
    • 10144225635 scopus 로고    scopus 로고
    • Self-interaction chromatography: a tool for the study of protein-protein interactions in bioprocessing environments
    • Patro S.Y., Przybycien T.M. Self-interaction chromatography: a tool for the study of protein-protein interactions in bioprocessing environments. Biotechnol. Bioeng. 1996, 52:193-203.
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 193-203
    • Patro, S.Y.1    Przybycien, T.M.2
  • 20
    • 0036194842 scopus 로고    scopus 로고
    • Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography
    • Tessier P.M., Lenhoff A.M., Sandler S.I. Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography. Biophys. J. 2002, 82:1620-1631.
    • (2002) Biophys. J. , vol.82 , pp. 1620-1631
    • Tessier, P.M.1    Lenhoff, A.M.2    Sandler, S.I.3
  • 21
    • 0034705635 scopus 로고    scopus 로고
    • Pore size distributions of cation exchange adsorbents determined by inverse size-exclusion chromatography
    • DePhillips P., Lenhoff A.M. Pore size distributions of cation exchange adsorbents determined by inverse size-exclusion chromatography. J. Chromatogr. A 2000, 883:39-54.
    • (2000) J. Chromatogr. A , vol.883 , pp. 39-54
    • DePhillips, P.1    Lenhoff, A.M.2
  • 22
    • 2342539781 scopus 로고    scopus 로고
    • Determination of pore size distributions of porous chromatographic adsorbents by inverse size-exclusion chromatography
    • Yao Y., Lenhoff A.M. Determination of pore size distributions of porous chromatographic adsorbents by inverse size-exclusion chromatography. J. Chromatogr. A 2004, 1037:273-282.
    • (2004) J. Chromatogr. A , vol.1037 , pp. 273-282
    • Yao, Y.1    Lenhoff, A.M.2
  • 23
    • 23044505404 scopus 로고    scopus 로고
    • Design of self-interaction chromatography as an analytical tool for predicting protein phase behavior
    • Ahamed T., Ottens M., van Dedem G.W.K., van der Wielen L.A.M. Design of self-interaction chromatography as an analytical tool for predicting protein phase behavior. J. Chromatogr. A 2005, 1089:111-124.
    • (2005) J. Chromatogr. A , vol.1089 , pp. 111-124
    • Ahamed, T.1    Ottens, M.2    van Dedem, G.W.K.3    van der Wielen, L.A.M.4
  • 24
    • 2942748360 scopus 로고    scopus 로고
    • Measurement of lysozyme-lysozyme interactions with quantitative affinity chromatography
    • Teske C.A., Blanch H.W., Prausnitz J.M. Measurement of lysozyme-lysozyme interactions with quantitative affinity chromatography. J. Phys. Chem. B 2004, 108:7437-7444.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 7437-7444
    • Teske, C.A.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 25
    • 35148854475 scopus 로고    scopus 로고
    • A simpler analysis for the measurement of second virial coefficients by self-interaction chromatography
    • Winzor D.J., Scott D.J., Wills P.R. A simpler analysis for the measurement of second virial coefficients by self-interaction chromatography. Anal. Biochem. 2007, 371:21-25.
    • (2007) Anal. Biochem. , vol.371 , pp. 21-25
    • Winzor, D.J.1    Scott, D.J.2    Wills, P.R.3
  • 27
    • 22744444652 scopus 로고    scopus 로고
    • The roles of additives and precipitants in crystallization of calcium- and integrin-binding protein
    • Berger B.W., Blamey C.J., Naik U.P., Bahnson B.J., Lenhoff A.M. The roles of additives and precipitants in crystallization of calcium- and integrin-binding protein. Cryst. Growth Des. 2005, 5:1499-1507.
    • (2005) Cryst. Growth Des. , vol.5 , pp. 1499-1507
    • Berger, B.W.1    Blamey, C.J.2    Naik, U.P.3    Bahnson, B.J.4    Lenhoff, A.M.5
  • 28
    • 28444457469 scopus 로고    scopus 로고
    • Second virial coefficient studies of cosolvent-induced protein self-interaction
    • Valente J.J., Verma K.S., Manning M.C., Wilson W.W., Henry C.S. Second virial coefficient studies of cosolvent-induced protein self-interaction. Biophys. J. 2005, 89:4211-4218.
    • (2005) Biophys. J. , vol.89 , pp. 4211-4218
    • Valente, J.J.1    Verma, K.S.2    Manning, M.C.3    Wilson, W.W.4    Henry, C.S.5
  • 29
    • 74549226587 scopus 로고    scopus 로고
    • Self-interaction chromatography as a tool for optimizing conditions for membrane protein crystallization
    • Gabrielsen M., Nagy L.A., DeLucas L.J., Cogdell R.J. Self-interaction chromatography as a tool for optimizing conditions for membrane protein crystallization. Acta Crystallogr. D: Biol. Crystallogr. 2010, 66:44-50.
    • (2010) Acta Crystallogr. D: Biol. Crystallogr. , vol.66 , pp. 44-50
    • Gabrielsen, M.1    Nagy, L.A.2    DeLucas, L.J.3    Cogdell, R.J.4
  • 32
    • 0142122294 scopus 로고    scopus 로고
    • Measurements of protein self-association as a guide to crystallization
    • Tessier P.M., Lenhoff A.M. Measurements of protein self-association as a guide to crystallization. Curr. Opin. Biotechnol. 2003, 14:512-516.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 512-516
    • Tessier, P.M.1    Lenhoff, A.M.2
  • 33
    • 58349084293 scopus 로고    scopus 로고
    • Self-interaction of native and denatured lysozyme in the presence of osmolytes, l-arginine and guanidine hydrochloride
    • Dong X.-Y., Liu J.-H., Liu F.-F., Sun Y. Self-interaction of native and denatured lysozyme in the presence of osmolytes, l-arginine and guanidine hydrochloride. Biochem. Eng. J. 2009, 43:321-326.
    • (2009) Biochem. Eng. J. , vol.43 , pp. 321-326
    • Dong, X.-Y.1    Liu, J.-H.2    Liu, F.-F.3    Sun, Y.4
  • 35
    • 0037359042 scopus 로고    scopus 로고
    • Screening of protein-ligand interactions by affinity chromatography
    • Garcia C.D., Holman S.C., Henry C.S., Wilson W.W. Screening of protein-ligand interactions by affinity chromatography. Biotechnol. Prog. 2003, 19:575-579.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 575-579
    • Garcia, C.D.1    Holman, S.C.2    Henry, C.S.3    Wilson, W.W.4
  • 36
    • 34548427923 scopus 로고    scopus 로고
    • Patterns of protein-protein interactions in salt solutions and implications for protein crystallization
    • Dumetz A.C., Snellinger-O'Brien A.M., Kaler E.W., Lenhoff A.M. Patterns of protein-protein interactions in salt solutions and implications for protein crystallization. Protein Sci. 2007, 16:1867-1877.
    • (2007) Protein Sci. , vol.16 , pp. 1867-1877
    • Dumetz, A.C.1    Snellinger-O'Brien, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 37
    • 0037782006 scopus 로고    scopus 로고
    • Measuring protein interactions by microchip self-interaction chromatography
    • Garcia C.D., Hadley D.J., Wilson W.W., Henry C.S. Measuring protein interactions by microchip self-interaction chromatography. Biotechnol. Prog. 2003, 19:1006-1010.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 1006-1010
    • Garcia, C.D.1    Hadley, D.J.2    Wilson, W.W.3    Henry, C.S.4
  • 38
    • 78649934968 scopus 로고    scopus 로고
    • Micro-fluidic device for measuring osmotic second virial coefficients
    • W.W. Wilson, C.S. Henry, C.D. Garcia, Micro-fluidic device for measuring osmotic second virial coefficients, US patent 6,974,678 (2005).
    • (2005) US patent , vol.6 , Issue.974 , pp. 678
    • Wilson, W.W.1    Henry, C.S.2    Garcia, C.D.3
  • 40
    • 0034604836 scopus 로고    scopus 로고
    • Physical evidence of two wall effects in liquid chromatography
    • Shalliker R.A., Broyles B.S., Guiochon G. Physical evidence of two wall effects in liquid chromatography. J. Chromatogr. A 2000, 888:1-12.
    • (2000) J. Chromatogr. A , vol.888 , pp. 1-12
    • Shalliker, R.A.1    Broyles, B.S.2    Guiochon, G.3
  • 41
    • 84859338859 scopus 로고
    • Continuous rods of macroporous polymer as high-performance liquid-chromatography separation media
    • Svec F., Frechet J.M.J. Continuous rods of macroporous polymer as high-performance liquid-chromatography separation media. Anal. Chem. 1992, 64:820-822.
    • (1992) Anal. Chem. , vol.64 , pp. 820-822
    • Svec, F.1    Frechet, J.M.J.2
  • 42
    • 33751157028 scopus 로고
    • Kinetic control of pore formation in macroporous polymers-formation of molded porous materials with high-flow characteristics for separations or catalysis
    • Svec F., Frechet J.M.J. Kinetic control of pore formation in macroporous polymers-formation of molded porous materials with high-flow characteristics for separations or catalysis. Chem. Mater. 1995, 7:707-715.
    • (1995) Chem. Mater. , vol.7 , pp. 707-715
    • Svec, F.1    Frechet, J.M.J.2
  • 43
    • 0037102287 scopus 로고    scopus 로고
    • Enzymatic microreactor-on-a-chip: protein mapping using trypsin immobilized on porous polymer monoliths molded in channels of microfluidic devices
    • Peterson D.S., Rohr T., Svec F., Frechet J.M.J. Enzymatic microreactor-on-a-chip: protein mapping using trypsin immobilized on porous polymer monoliths molded in channels of microfluidic devices. Anal. Chem. 2002, 74:4081-4088.
    • (2002) Anal. Chem. , vol.74 , pp. 4081-4088
    • Peterson, D.S.1    Rohr, T.2    Svec, F.3    Frechet, J.M.J.4
  • 44
    • 0142135898 scopus 로고    scopus 로고
    • Dual-function microanalytical device by in situ photolithographic grafting of porous polymer monolith: integrating solid-phase extraction and enzymatic digestion for peptide mass mapping
    • Peterson D.S., Rohr T., Svec F., Frechet J.M.J. Dual-function microanalytical device by in situ photolithographic grafting of porous polymer monolith: integrating solid-phase extraction and enzymatic digestion for peptide mass mapping. Anal. Chem. 2003, 75:5328-5335.
    • (2003) Anal. Chem. , vol.75 , pp. 5328-5335
    • Peterson, D.S.1    Rohr, T.2    Svec, F.3    Frechet, J.M.J.4
  • 45
    • 34548558873 scopus 로고    scopus 로고
    • Photopatterning enzymes on polymer monoliths in microfluidic devices for steady-state kinetic analysis and spatially separated multi-enzyme reactions
    • Logan T.C., Clark D.S., Stachowiak T.B., Svec F., Frechet J.M.J. Photopatterning enzymes on polymer monoliths in microfluidic devices for steady-state kinetic analysis and spatially separated multi-enzyme reactions. Anal. Chem. 2007, 79:6592-6598.
    • (2007) Anal. Chem. , vol.79 , pp. 6592-6598
    • Logan, T.C.1    Clark, D.S.2    Stachowiak, T.B.3    Svec, F.4    Frechet, J.M.J.5
  • 46
    • 0037432370 scopus 로고    scopus 로고
    • Photografting and the control of surface chemistry in three-dimensional porous polymer monoliths
    • Rohr T., Hilder E.F., Donovan J.J., Svec F., Frechet J.M.J. Photografting and the control of surface chemistry in three-dimensional porous polymer monoliths. Macromolecules 2003, 36:1677-1684.
    • (2003) Macromolecules , vol.36 , pp. 1677-1684
    • Rohr, T.1    Hilder, E.F.2    Donovan, J.J.3    Svec, F.4    Frechet, J.M.J.5
  • 47
    • 33846138950 scopus 로고    scopus 로고
    • Patternable protein resistant surfaces for multifunctional microfluidic devices via surface hydrophilization of porous polymer monoliths using photografting
    • Stachowiak T.B., Svec F., Frechet J.M.J. Patternable protein resistant surfaces for multifunctional microfluidic devices via surface hydrophilization of porous polymer monoliths using photografting. Chem. Mater. 2006, 18:5950-5957.
    • (2006) Chem. Mater. , vol.18 , pp. 5950-5957
    • Stachowiak, T.B.1    Svec, F.2    Frechet, J.M.J.3
  • 48
    • 33845893020 scopus 로고    scopus 로고
    • Stability and repeatability of capillary columns based on porous monoliths of poly(butyl methacrylate-co-ethylene dimethacrylate)
    • Geiser L., Eeltink S., Svec F., Frechet J.M.J. Stability and repeatability of capillary columns based on porous monoliths of poly(butyl methacrylate-co-ethylene dimethacrylate). J. Chromatogr. A 2007, 1140:140-146.
    • (2007) J. Chromatogr. A , vol.1140 , pp. 140-146
    • Geiser, L.1    Eeltink, S.2    Svec, F.3    Frechet, J.M.J.4
  • 50
    • 4344647040 scopus 로고    scopus 로고
    • Preparation and HPLC applications of rigid macroporous organic polymer monoliths
    • Svec F. Preparation and HPLC applications of rigid macroporous organic polymer monoliths. J. Sep. Sci. 2004, 27:747-766.
    • (2004) J. Sep. Sci. , vol.27 , pp. 747-766
    • Svec, F.1
  • 51
    • 0033879098 scopus 로고    scopus 로고
    • A novel sequential photoinduced living graft polymerization
    • Ma H.M., Davis R.H., Bowman C.N. A novel sequential photoinduced living graft polymerization. Macromolecules 2000, 33:331-335.
    • (2000) Macromolecules , vol.33 , pp. 331-335
    • Ma, H.M.1    Davis, R.H.2    Bowman, C.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.