메뉴 건너뛰기




Volumn 27, Issue 5, 2011, Pages 1830-1836

Protein-associated water and secondary structure effect removal of blood proteins from metallic substrates

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION ENERGY; ADHESION FORCES; ADSORBED AMOUNT; ADSORBED LAYERS; ADSORPTION STUDIES; ALKALINE SOLUTIONS; AU SURFACES; BLOOD PROTEIN; BOVINE SERUM ALBUMINS; CLEAN METAL; CLEANING SOLUTION; DISSIPATION MEASUREMENTS; GLOBULAR PROTEINS; HIGH-RESOLUTION MEASUREMENTS; HYDROPHOBIC INTERACTIONS; METAL SUBSTRATE; METAL SURFACES; METALLIC SUBSTRATE; NATIVE OXIDES; PLATINUM AND GOLD; POLYMERIC SUBSTRATE; PROTEIN ADSORPTION; PROTEIN LAYERS; PROTEIN STRUCTURES; PROTEIN-PROTEIN INTERACTIONS; PROTEIN-SURFACE INTERACTIONS; QUARTZ CRYSTAL MICROBALANCE WITH DISSIPATION; REMOVAL EFFICIENCIES; SECONDARY STRUCTURE OF PROTEINS; SECONDARY STRUCTURES; SHIP OWNERS; STRUCTURAL CONTENT; SURFACE FOULING; SURFACE PLASMON RESONANCE SPECTROSCOPY; SURFACTANT SOLUTION; SURGICAL INSTRUMENT; WATER COMPLEXES;

EID: 79951865359     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la1041794     Document Type: Article
Times cited : (37)

References (64)
  • 1
    • 65249175791 scopus 로고    scopus 로고
    • How Interfaces Affect Hydrophobically Driven Polymer Folding
    • Jamadagni, S. N.; Godawat, R.; Dordick, J. S.; Garde, S. How Interfaces Affect Hydrophobically Driven Polymer Folding J. Phys. Chem. B 2009, 113 (13) 4093-4101
    • (2009) J. Phys. Chem. B , vol.113 , Issue.13 , pp. 4093-4101
    • Jamadagni, S.N.1    Godawat, R.2    Dordick, J.S.3    Garde, S.4
  • 3
    • 0037422948 scopus 로고    scopus 로고
    • Irreversibility and polymer adsorption
    • O-Shaughnessy, B.; Vavylonis, D. Irreversibility and polymer adsorption Phys. Rev. Lett. 2003, 90 (5) 056103
    • (2003) Phys. Rev. Lett. , vol.90 , Issue.5 , pp. 056103
    • Oshaughnessy, B.1    Vavylonis, D.2
  • 4
    • 0029200584 scopus 로고
    • The influence of micro-topography on cellular-response and the implications for silicone implants
    • Vonrecum, A. F.; Vankooten, T. G. The influence of micro-topography on cellular-response and the implications for silicone implants J. Biomater. Sci., Polym. Ed. 1995, 7 (2) 181-198
    • (1995) J. Biomater. Sci., Polym. Ed. , vol.7 , Issue.2 , pp. 181-198
    • Vonrecum, A.F.1    Vankooten, T.G.2
  • 5
    • 33748537017 scopus 로고    scopus 로고
    • Adsorption kinetics of an engineered gold binding peptide by surface plasmon resonance spectroscopy and a quartz crystal microbalance
    • DOI 10.1021/la0606897
    • Tamerler, C.; Oren, E. E.; Duman, M.; Venkatasubramanian, E.; Sarikaya, M. Adsorption kinetics of an engineered gold binding peptide by surface plasmon resonance spectroscopy and a quartz crystal microbalance Langmuir 2006, 22 (18) 7712-7718 (Pubitemid 44373445)
    • (2006) Langmuir , vol.22 , Issue.18 , pp. 7712-7718
    • Tamerler, C.1    Oren, E.E.2    Duman, M.3    Venkatasubramanian, E.4    Sarikaya, M.5
  • 6
    • 0344584917 scopus 로고    scopus 로고
    • Nanometer-scale roughness having little effect on the amount or structure of adsorbed protein
    • Han, M.; Sethuraman, A.; Kane, R. S.; Belfort, G. Nanometer-scale roughness having little effect on the amount or structure of adsorbed protein Langmuir 2003, 19 (23) 9868-9872
    • (2003) Langmuir , vol.19 , Issue.23 , pp. 9868-9872
    • Han, M.1    Sethuraman, A.2    Kane, R.S.3    Belfort, G.4
  • 7
    • 0028524562 scopus 로고
    • Immobilization of silver and platinum ions for metal affinity- chromatography
    • Garcia, A. A.; Kim, D. H.; Miles, D. R. Immobilization of silver and platinum ions for metal affinity-chromatography React. Polym. 1994, 23 (2-3) 249-259
    • (1994) React. Polym. , vol.23 , Issue.3 , pp. 249-259
    • Garcia, A.A.1    Kim, D.H.2    Miles, D.R.3
  • 8
    • 0031677471 scopus 로고    scopus 로고
    • Comparison of Retention and Binding Behavior of dUTP and Biotin-Conjugated dUTP Using an Immobilized Silver Ion Chromatography Support
    • Agarwal, S.; Garcia, A. A.; Miles, D. Comparison of retention and binding behavior of dUTP and biotin-conjugated dUTP using an immobilized silver ion chromatography support Sep. Sci. Technol. 1998, 33 (1) 1-18 (Pubitemid 128499279)
    • (1998) Separation Science and Technology , vol.33 , Issue.1 , pp. 1-18
    • Agarwal, S.1    Garcia, A.A.2    Miles, D.3
  • 9
    • 0028764674 scopus 로고
    • Protein fractionation using fast flow immobilized metal chelate affinity membranes
    • DOI 10.1002/bit.260430105
    • Serafica, G. C.; Belfort, G.; Pimbley, J. Protein fractionation using fast flow immobilized metal chelate affinity membranes Biotechnol. Bioeng. 1994, 43 (1) 21-36 (Pubitemid 24001733)
    • (1994) Biotechnology and Bioengineering , vol.43 , Issue.1 , pp. 21-36
    • Serafica, G.C.1    Pimbley, J.2    Belfort, G.3
  • 10
    • 0035797979 scopus 로고    scopus 로고
    • Self-assembled monolayers that resist the adsorption of proteins and the adhesion of bacterial and mammalian cells
    • DOI 10.1021/la010552a
    • Ostuni, E.; Chapman, R. G.; Liang, M. N.; Meluleni, G.; Pier, G.; Ingber, D. E.; Whitesides, G. M. Self-Assembled Monolayers That Resist the Adsorption of Proteins and the Adhesion of Bacterial and Mammalian Cells Langmuir 2001, 17 (20) 6336-6343 (Pubitemid 35330713)
    • (2001) Langmuir , vol.17 , Issue.20 , pp. 6336-6343
    • Ostuni, E.1    Chapman, R.G.2    Liang, M.N.3    Meluleni, G.4    Pier, G.5    Ingber, D.E.6    Whitesides, G.M.7
  • 11
    • 4444293962 scopus 로고    scopus 로고
    • Effect of surface wettability on the adhesion of proteins
    • Sethuraman, A.; Han, M.; Kane, R. S.; Belfort, G. Effect of surface wettability on the adhesion of proteins Langmuir 2004, 20 (18) 7779-88
    • (2004) Langmuir , vol.20 , Issue.18 , pp. 7779-88
    • Sethuraman, A.1    Han, M.2    Kane, R.S.3    Belfort, G.4
  • 14
    • 0345688752 scopus 로고    scopus 로고
    • Influence of hydrophobic teflon particles on the structure of amyloid β-peptide
    • DOI 10.1021/bm034151g
    • Giacomelli, C. E.; Norde, W. Influence of hydrophobic Teflon particles on the structure of amyloid beta-peptide Biomacromolecules 2003, 4 (6) 1719-1726 (Pubitemid 37455585)
    • (2003) Biomacromolecules , vol.4 , Issue.6 , pp. 1719-1726
    • Giacomelli, C.E.1    Norde, W.2
  • 16
    • 0031574008 scopus 로고    scopus 로고
    • Adsorption-induced conformational changes in the serine proteinase savinase: A tryptophan fluorescence and circular dichroism study
    • DOI 10.1006/jcis.1997.5205
    • Maste, M. C. L.; Norde, W.; Visser, A. J. W. G. Adsorption-induced conformational changes in the serine proteinase savinase: A tryptophan fluorescence and circular dichroism study J. Colloid Interface Sci. 1997, 196 (2) 224-230 (Pubitemid 28080785)
    • (1997) Journal of Colloid and Interface Science , vol.196 , Issue.2 , pp. 224-230
    • Maste, M.C.L.1    Norde, W.2    Visser, A.J.W.G.3
  • 17
    • 0033275324 scopus 로고    scopus 로고
    • Conformational changes in proteins at interfaces: From solution to the interface, and back
    • Norde, W.; Giacomelli, C. E. Conformational changes in proteins at interfaces: from solution to the interface, and back Macromol. Symp. 1999, 145, 125-136 (Pubitemid 129655193)
    • (1999) Macromolecular Symposia , vol.145 , pp. 125-136
    • Norde, W.1    Giacomelli, C.E.2
  • 18
    • 36649017886 scopus 로고    scopus 로고
    • Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes
    • DOI 10.1021/la702091c
    • Asuri, P.; Bale, S. S.; Pangule, R. C.; Shah, D. A.; Kane, R. S.; Dordick, J. S. Structure, Function, and Stability of Enzymes Covalently Attached to Single-Walled Carbon Nanotubes Langmuir 2007, 23 (24) 12318-12321 (Pubitemid 350197408)
    • (2007) Langmuir , vol.23 , Issue.24 , pp. 12318-12321
    • Asuri, P.1    Bale, S.S.2    Pangule, R.C.3    Shah, D.A.4    Kane, R.S.5    Dordick, J.S.6
  • 19
    • 22444440762 scopus 로고    scopus 로고
    • Functional monolayers for improved resistance to protein adsorption: Oligo(ethylene glycol)-modified silicon and diamond surfaces
    • DOI 10.1021/la050362q
    • Clare, T. L.; Clare, B. H.; Nichols, B. M.; Abbott, N. L.; Hamers, R. J. Functional monolayers for improved resistance to protein adsorption: Oligo(ethylene glycol)-modified silicon and diamond surfaces Langmuir 2005, 21 (14) 6344-6355 (Pubitemid 41006449)
    • (2005) Langmuir , vol.21 , Issue.14 , pp. 6344-6355
    • Clare, T.L.1    Clare, B.H.2    Nichols, B.M.3    Abbott, N.L.4    Hamers, R.J.5
  • 20
    • 11144230048 scopus 로고    scopus 로고
    • Structure and function of enzymes adsorbed onto single-walled carbon nanotubes
    • DOI 10.1021/la047994h
    • Karajanagi, S. S.; Vertegel, A. A.; Kane, R. S.; Dordick, J. S. Structure and function of enzymes adsorbed onto single-walled carbon nanotubes Langmuir 2004, 20 (26) 11594-11599 (Pubitemid 40049633)
    • (2004) Langmuir , vol.20 , Issue.26 , pp. 11594-11599
    • Karajanagi, S.S.1    Vertegel, A.A.2    Kane, R.S.3    Dordick, J.S.4
  • 21
    • 0002990922 scopus 로고    scopus 로고
    • Functionalization of Carbon Nanotubes for Biocompatibility and Biomolecular Recognition
    • DOI 10.1021/nl015692j
    • Shim, M.; Kam, N. W. S.; Chen, R. J.; Li, Y. M.; Dai, H. J. Functionalization of carbon nanotubes for biocompatibility and biomolecular recognition Nano Lett. 2002, 2 (4) 285-288 (Pubitemid 135706308)
    • (2002) Nano Letters , vol.2 , Issue.4 , pp. 285-288
    • Shim, M.1    Kam, N.W.S.2    Chen, R.J.3    Li, Y.4    Dai, H.5
  • 23
    • 0020716183 scopus 로고
    • Protein adsorption and desorption phenomena on clean metal surfaces
    • DOI 10.1002/jbm.820190312
    • Williams, D. F.; Askill, I. N.; Smith, R. Protein adsorption and desorption phenomena on clean metal surfaces J. Biomed. Mater. Res. 1985, 19 (3) 313-320 (Pubitemid 15101374)
    • (1985) Journal of Biomedical Materials Research , vol.19 , Issue.3 , pp. 313-320
    • Williams, D.F.1    Askill, I.N.2    Smith, R.3
  • 24
    • 79951864725 scopus 로고    scopus 로고
    • Modeling of Protein Adsorption on a Metal Surface: Brownian Dynamics Simulations
    • Kokh, D. B.; Huang, B.; Wade, R. C.; Winn, P. J. Modeling of Protein Adsorption on a Metal Surface: Brownian Dynamics Simulations Biophys. J. 2009, 96 (3, Suppl. 1) 298a-299a
    • (2009) Biophys. J. , vol.96 , Issue.SUPPL. 1
    • Kokh, D.B.1    Huang, B.2    Wade, R.C.3    Winn, P.J.4
  • 26
    • 0034762389 scopus 로고    scopus 로고
    • Presence of protein deposits on 'cleaned' re-usable anaesthetic equipment
    • DOI 10.1046/j.1365-2044.2001.02277.x
    • Miller, D. M.; Youkhana, I.; Karunaratne, W. U.; Pearce, A. Presence of protein deposits on -cleaned- re-usable anaesthetic equipment Anaesthesia 2001, 56 (11) 1069-72 (Pubitemid 33039933)
    • (2001) Anaesthesia , vol.56 , Issue.11 , pp. 1069-1072
    • Miller, D.M.1    Youkhana, I.2    Karunaratne, W.U.3    Pearce, A.4
  • 31
    • 60549087904 scopus 로고    scopus 로고
    • Multivalency-Assisted Control of Intracellular Signaling Pathways: Application for Ubiquitin-Dependent N-End Rule Pathway
    • Sriram, S. M.; Banerjee, R.; Kane, R. S.; Kwon, Y. T. Multivalency-Assisted Control of Intracellular Signaling Pathways: Application for Ubiquitin-Dependent N-End Rule Pathway Chem. Biol. 2009, 16 (2) 121-131
    • (2009) Chem. Biol. , vol.16 , Issue.2 , pp. 121-131
    • Sriram, S.M.1    Banerjee, R.2    Kane, R.S.3    Kwon, Y.T.4
  • 32
    • 0348044405 scopus 로고    scopus 로고
    • Smooth model cellulose I surfaces from nanocrystal suspensions
    • DOI 10.1023/A:1027333928715
    • Edgar, C. D.; Gray, D. G. Smooth model cellulose I surfaces from nanocrystal suspensions Cellulose 2003, 10 (4) 299-306 (Pubitemid 37529412)
    • (2003) Cellulose , vol.10 , Issue.4 , pp. 299-306
    • Edgar, C.D.1    Gray, D.G.2
  • 33
    • 36449007442 scopus 로고
    • Calibration of atomic-force microscope tips
    • Hutter, J. L.; Bechhoefer, J. Calibration of atomic-force microscope tips Rev. Sci. Instrum. 1993, 64 (7) 1868-73
    • (1993) Rev. Sci. Instrum. , vol.64 , Issue.7 , pp. 1868-73
    • Hutter, J.L.1    Bechhoefer, J.2
  • 34
    • 0010461312 scopus 로고
    • Untersuchungen über die Reibung und Adhäsion (Investigations over the friction and adhesion)
    • Derjaguin, B. V. Untersuchungen über die Reibung und Adhäsion (Investigations over the friction and adhesion) Kolloid Z. 1934, 69, 155-164
    • (1934) Kolloid Z. , vol.69 , pp. 155-164
    • Derjaguin, B.V.1
  • 35
    • 0001366447 scopus 로고
    • Determination of the isoelectric points of several metals by an adhesion method
    • Kallay, N.; Torbic, Z.; Golic, M.; Matijevic, E. Determination of the isoelectric points of several metals by an adhesion method J. Phys. Chem. 1991, 95 (18) 7028-7032
    • (1991) J. Phys. Chem. , vol.95 , Issue.18 , pp. 7028-7032
    • Kallay, N.1    Torbic, Z.2    Golic, M.3    Matijevic, E.4
  • 36
    • 67651151037 scopus 로고    scopus 로고
    • Determination of isoelectric points of metals and metallic alloys by adhesion of latex particles
    • Lefèvre, G.; Cerovic, L.; Milonjic, S.; Fédoroff, M.; Finne, J.; Jaubertie, A. Determination of isoelectric points of metals and metallic alloys by adhesion of latex particles J. Colloid Interface Sci. 2009, 337 (2) 449-455
    • (2009) J. Colloid Interface Sci. , vol.337 , Issue.2 , pp. 449-455
    • Lefèvre, G.1    Cerovic, L.2    Milonjic, S.3    Fédoroff, M.4    Finne, J.5    Jaubertie, A.6
  • 37
    • 33745028618 scopus 로고    scopus 로고
    • Particle surface properties of stainless steel-coated tungsten carbide powders
    • DOI 10.1016/j.powtec.2006.03.005, PII S0032591006000921
    • Fernandes, C. M.; Senos, A. M. R.; Vieira, M. T. Particle surface properties of stainless steel-coated tungsten carbide powders Powder Technol. 2006, 164 (3) 124-129 (Pubitemid 43870361)
    • (2006) Powder Technology , vol.164 , Issue.3 , pp. 124-129
    • Fernandes, C.M.1    Senos, A.M.R.2    Vieira, M.T.3
  • 39
    • 28844458899 scopus 로고
    • Isoelectric points of solid oxides solid hydroxides and aqueous hydroxo complex systems
    • Parks, G. A. Isoelectric points of solid oxides solid hydroxides and aqueous hydroxo complex systems Chem. Rev. 1965, 65 (2) 177
    • (1965) Chem. Rev. , vol.65 , Issue.2 , pp. 177
    • Parks, G.A.1
  • 40
    • 0345148822 scopus 로고    scopus 로고
    • An experimental study of the stability of TiO2 particles in organic-water mixtures
    • Hsu, J.-P.; Chang, Y.-T. An experimental study of the stability of TiO2 particles in organic-water mixtures Colloids Surf., A 2000, 161 (3) 423-437
    • (2000) Colloids Surf., A , vol.161 , Issue.3 , pp. 423-437
    • Hsu, J.-P.1    Chang, Y.-T.2
  • 41
    • 0020808361 scopus 로고
    • DIRECT METHOD FOR STUDYING PARTICLE DEPOSITION ONTO SOLID SURFACES
    • Dabros, T.; van de Ven, T. G. M. A Direct Method for Studying Particle Deposition onto Solid Surfaces Colloid Polym. Sci. 1983, 261, 694-707 (Pubitemid 14453079)
    • (1983) Colloid and Polymer Science , vol.261 , Issue.8 , pp. 694-707
    • Dabros, T.1    Van De Ven, T.G.M.2
  • 42
    • 84951279351 scopus 로고
    • Venvendung von Schwingquarzen sur Wagung Dunner Schichten und zur Mikrowagung -Translation - Use of vibrating quartz for weighing of thin layers and for microweighing
    • Sauerbrey, G. Venvendung von Schwingquarzen sur Wagung Dunner Schichten und zur Mikrowagung -Translation-Use of vibrating quartz for weighing of thin layers and for microweighing Z. Phys. A: Hadrons Nucl. 1959, 155 (2) 206-222
    • (1959) Z. Phys. A: Hadrons Nucl. , vol.155 , Issue.2 , pp. 206-222
    • Sauerbrey, G.1
  • 43
    • 0032317747 scopus 로고    scopus 로고
    • The removal of β-lactoglobulin from stainless steel surfaces at high and low temperature as influenced by the type and concentration of cleaning agent
    • Karlsson, C. A. C.; Wahlgren, M. C.; Tragardh, A. C. The removal of beta-lactoglobulin from stainless steel surfaces at high and low temperature as influenced by the type and concentration of cleaning agent J. Food Process Eng. 1998, 21 (6) 485-501 (Pubitemid 128653617)
    • (1998) Journal of Food Process Engineering , vol.21 , Issue.6 , pp. 485-501
    • Karlsson, C.A.-C.1    Wahlgren, M.C.2    Tragardh, A.C.3
  • 44
    • 49149124256 scopus 로고    scopus 로고
    • In-depth investigation of protein adsorption on gold surfaces: Correlating the structure and density to the efficiency of the sensing layer
    • Boujday, S.; Bantegnie, A.; Briand, E.; Marnet, P. G.; Salmain, M.; Pradier, C. M. In-depth investigation of protein adsorption on gold surfaces: Correlating the structure and density to the efficiency of the sensing layer J. Phys. Chem. B 2008, 112 (21) 6708-6715
    • (2008) J. Phys. Chem. B , vol.112 , Issue.21 , pp. 6708-6715
    • Boujday, S.1    Bantegnie, A.2    Briand, E.3    Marnet, P.G.4    Salmain, M.5    Pradier, C.M.6
  • 45
    • 58249132928 scopus 로고    scopus 로고
    • Interactions between polycationic and polyanionic layers: Changes in rigidity, charge and adsorption kinetics
    • Dutta, A. K.; Belfort, G. Interactions between polycationic and polyanionic layers: Changes in rigidity, charge and adsorption kinetics Sens. Actuators, B 2009, 136 (1) 60-65
    • (2009) Sens. Actuators, B , vol.136 , Issue.1 , pp. 60-65
    • Dutta, A.K.1    Belfort, G.2
  • 46
    • 38949165048 scopus 로고    scopus 로고
    • Reversibly controlling the rigidity of adsorbed polycations
    • DOI 10.1021/ma071608w
    • Dutta, A. K.; Nayak, A.; Belfort, G. Reversibly Controlling the Rigidity of Adsorbed Polycations Macromolecules 2007, 41 (2) 301-304 (Pubitemid 351212622)
    • (2008) Macromolecules , vol.41 , Issue.2 , pp. 301-304
    • Dutta, A.K.1    Nayak, A.2    Belfort, G.3
  • 48
    • 55549139118 scopus 로고    scopus 로고
    • QCM-D sensitivity to protein adsorption reversibility
    • Jordan, J. L.; Fernandez, E. J. QCM-D sensitivity to protein adsorption reversibility Biotechnol. Bioeng. 2008, 101 (4) 837-842
    • (2008) Biotechnol. Bioeng. , vol.101 , Issue.4 , pp. 837-842
    • Jordan, J.L.1    Fernandez, E.J.2
  • 49
    • 0028939393 scopus 로고
    • Interfacial activation-based molecular bioimprinting of lipolytic enzymes
    • Mingarro, I.; Abad, C.; Braco, L. Interfacial activation-based molecular bioimprinting of lipolytic enzymes Proc. Natl. Acad. Sci. U.S.A. 1995, 92 (8) 3308-3312
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , Issue.8 , pp. 3308-3312
    • Mingarro, I.1    Abad, C.2    Braco, L.3
  • 50
    • 34250325895 scopus 로고    scopus 로고
    • QCM-D real-time monitoring of structural changes in an adsorbed protein layer
    • Zelander, G. QCM-D real-time monitoring of structural changes in an adsorbed protein layer Nature Methods 2006, 41-42
    • (2006) Nature Methods , pp. 41-42
    • Zelander, G.1
  • 51
    • 66149088055 scopus 로고    scopus 로고
    • Stability of Tethered Proteins
    • Anand, G.; Sharma, S.; Kumar, S. K.; Belfort, G. Stability of Tethered Proteins Langmuir 2009, 25 (9) 4998-5005
    • (2009) Langmuir , vol.25 , Issue.9 , pp. 4998-5005
    • Anand, G.1    Sharma, S.2    Kumar, S.K.3    Belfort, G.4
  • 52
    • 0032122890 scopus 로고    scopus 로고
    • Molecular packing of HSA, IgG, and fibrinogen adsorbed on silicon by AFM imaging
    • Ortega-Vinuesa, J. L.; Tengvall, P.; Lundström, I. Molecular packing of HSA, IgG, and fibrinogen adsorbed on silicon by AFM imaging Thin Solid Films 1998, 324 (1-2) 257-273 (Pubitemid 128442153)
    • (1998) Thin Solid Films , vol.324 , Issue.1-2 , pp. 257-273
    • Ortega-Vinuesa, J.L.1    Tengvall, P.2    Lundstrom, I.3
  • 53
    • 42549147441 scopus 로고    scopus 로고
    • Effect of solution pH on protein transmission and membrane capacity during virus filtration
    • DOI 10.1002/bit.21735
    • Bakhshayeshi, M.; Zydney, A. L. Effect of solution pH on protein transmission and membrane capacity during virus filtration Biotechnol. Bioeng. 2008, 100 (1) 108-117 (Pubitemid 351579021)
    • (2008) Biotechnology and Bioengineering , vol.100 , Issue.1 , pp. 108-117
    • Bakhshayeshi, M.1    Zydney, A.L.2
  • 54
    • 0035281198 scopus 로고    scopus 로고
    • The Interaction between SDS and Lysozyme at the Hydrophilic Solidâ-Water Interface
    • Green, R. J.; Su, T. J.; Lu, J. R.; Penfold, J. The Interaction between SDS and Lysozyme at the Hydrophilic Solidâ-Water Interface J. Phys. Chem. B 2001, 105 (8) 1594-1602
    • (2001) J. Phys. Chem. B , vol.105 , Issue.8 , pp. 1594-1602
    • Green, R.J.1    Su, T.J.2    Lu, J.R.3    Penfold, J.4
  • 55
    • 77954293169 scopus 로고    scopus 로고
    • Conformational Transitions of Adsorbed Proteins on Surfaces of Varying Polarity
    • Anand, G.; Sharma, S.; Dutta, A. K.; Kumar, S. K.; Belfort, G. Conformational Transitions of Adsorbed Proteins on Surfaces of Varying Polarity. Langmuir 26 (13), 10803 - 10811.
    • Langmuir , vol.26 , Issue.13 , pp. 10803-10811
    • Anand, G.1    Sharma, S.2    Dutta, A.K.3    Kumar, S.K.4    Belfort, G.5
  • 56
    • 0029913144 scopus 로고    scopus 로고
    • Multipoint binding in metal-affinity chromatography II. Effect of pH and imidazole on chromatographic retention of engineered histidine-containing cytochromes c
    • Johnson, R. D.; Todd, R. J.; Arnold, F. H. Multipoint binding in metal-affinity chromatography II. Effect of pH and imidazole on chromatographic retention of engineered histidine-containing cytochromes c J. Chromatogr., A 1996, 725 (2) 225-235
    • (1996) J. Chromatogr., A , vol.725 , Issue.2 , pp. 225-235
    • Johnson, R.D.1    Todd, R.J.2    Arnold, F.H.3
  • 58
    • 0030077272 scopus 로고    scopus 로고
    • A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance
    • Sigal, G. B.; Bamdad, C.; Barberis, A.; Strominger, J.; Whitesides, G. M. A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance Anal. Chem. 1996, 68 (3) 490-7
    • (1996) Anal. Chem. , vol.68 , Issue.3 , pp. 490-7
    • Sigal, G.B.1    Bamdad, C.2    Barberis, A.3    Strominger, J.4    Whitesides, G.M.5
  • 59
    • 0001586746 scopus 로고
    • Linkage isomerism in square-planar complexes of platinum and palladium with histidine and derivatives
    • Appleton, T. G.; Pesch, F. J.; Wienken, M.; Menzer, S.; Lippert, B. Linkage isomerism in square-planar complexes of platinum and palladium with histidine and derivatives Inorg. Chem. 1992, 31 (21) 4410-4419
    • (1992) Inorg. Chem. , vol.31 , Issue.21 , pp. 4410-4419
    • Appleton, T.G.1    Pesch, F.J.2    Wienken, M.3    Menzer, S.4    Lippert, B.5
  • 60
    • 0026722972 scopus 로고
    • Methionine and histidine Pd(II) and Pt(II) complexes - Crystal-structures and spectroscopic properties
    • Caubet, A.; Moreno, V.; Molins, E.; Miravitlles, C. Methionine and histidine Pd(II) and Pt(II) complexes-crystal-structures and spectroscopic properties J. Inorg. Biochem. 1992, 48 (2) 135-152
    • (1992) J. Inorg. Biochem. , vol.48 , Issue.2 , pp. 135-152
    • Caubet, A.1    Moreno, V.2    Molins, E.3    Miravitlles, C.4
  • 62
    • 0026118420 scopus 로고
    • Protein - Surface interactions in the presence of polyethylene oxide: II. Effect of protein size
    • Jeon, S. I.; Andrade, J. D. Protein - surface interactions in the presence of polyethylene oxide: II. Effect of protein size J. Colloid Interface Sci. 1991, 142 (1) 159-166
    • (1991) J. Colloid Interface Sci. , vol.142 , Issue.1 , pp. 159-166
    • Jeon, S.I.1    Andrade, J.D.2
  • 63
    • 0026122420 scopus 로고
    • Protein - Surface interactions in the presence of polyethylene oxide: I. Simplified theory
    • Jeon, S. I.; Lee, J. H.; Andrade, J. D.; De Gennes, P. G. Protein - surface interactions in the presence of polyethylene oxide: I. Simplified theory J. Colloid Interface Sci. 1991, 142 (1) 149-158
    • (1991) J. Colloid Interface Sci. , vol.142 , Issue.1 , pp. 149-158
    • Jeon, S.I.1    Lee, J.H.2    Andrade, J.D.3    De Gennes, P.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.