메뉴 건너뛰기




Volumn 4, Issue , 2006, Pages 614-618

Structure analysis of immobilized-bovine serum albumin by means of TOF-SIMS

Author keywords

Albumin; Structure analysis; Surface analysis; TOF SIMS

Indexed keywords

AMINO ACIDS; INDIUM COMPOUNDS; MOLECULAR STRUCTURE; SECONDARY ION MASS SPECTROMETRY; SURFACE REACTIONS;

EID: 33748262817     PISSN: 13480391     EISSN: 13480391     Source Type: Journal    
DOI: 10.1380/ejssnt.2006.614     Document Type: Article
Times cited : (8)

References (33)
  • 1
    • 33645381298 scopus 로고    scopus 로고
    • Protein and peptide arrays: Recent trends and new directions
    • M. Cretich, F. Damin, G. Pirri, M. Chiari, Protein and peptide arrays: Recent trends and new directions, Biomol. Eng. 23, 77-88 (2006).
    • (2006) Biomol. Eng. , vol.23 , pp. 77-88
    • Cretich, M.1    Damin, F.2    Pirri, G.3    Chiari, M.4
  • 2
    • 11944253040 scopus 로고    scopus 로고
    • Nanoanalytical measurement of protein orientation on conductive sensor surfaces
    • G. M. Hawlliwell, Nanoanalytical measurement of protein orientation on conductive sensor surfaces, Analyst 129, 1166-1170 (2004).
    • (2004) Analyst , vol.129 , pp. 1166-1170
    • Hawlliwell, G.M.1
  • 3
    • 33645514620 scopus 로고    scopus 로고
    • Quantitative mapping of the orientation of Fibroin β-sheets in B. mori cocoon fibers by scanning transmission X-ray microscopy
    • D. H. Cruz, M.-E. Rousseau, M. M. West, M. Pézolet, A. P. Hitchcock, Quantitative mapping of the orientation of Fibroin β-sheets in B. mori cocoon fibers by scanning transmission X-ray microscopy, Biomacromol. 7, 836-843 (2006).
    • (2006) Biomacromol. , vol.7 , pp. 836-843
    • Cruz, D.H.1    Rousseau, M.-E.2    West, M.M.3    Pézolet, M.4    Hitchcock, A.P.5
  • 4
    • 32044452254 scopus 로고    scopus 로고
    • Indole ring orientations of Trp 189 in the ground and M intermediate states of bacteriohodospin as studied by polarized UV resonance Raman spectroscopy
    • K. Asakawa, S. Masuda, H. Takeuchi, Indole ring orientations of Trp 189 in the ground and M intermediate states of bacteriohodospin as studied by polarized UV resonance Raman spectroscopy, J. Raman Spectrosc. 37, 255-262 (2006).
    • (2006) J. Raman Spectrosc. , vol.37 , pp. 255-262
    • Asakawa, K.1    Masuda, S.2    Takeuchi, H.3
  • 5
    • 12544256424 scopus 로고    scopus 로고
    • Chemical imaging the distribution of ions and molecules in developing and mature wheat grain
    • E. N. C. Mills, M. L. Parker, N. Wellner, G. Toole, K. Feeney, P. R. Shewry, Chemical imaging the distribution of ions and molecules in developing and mature wheat grain, J. Cereal Sci. 41, 193-201 (2005).
    • (2005) J. Cereal Sci. , vol.41 , pp. 193-201
    • Mills, E.N.C.1    Parker, M.L.2    Wellner, N.3    Toole, G.4    Feeney, K.5    Shewry, P.R.6
  • 6
    • 1942470540 scopus 로고    scopus 로고
    • Mapping the toporogy and determination of a low-resolution three-dimensional structure of the calmodulin-melittin complex by chemical cross-linking and high-resolution FTICRMS: Direct demonstration of multiple binding modes
    • D. M. Schulz, C. Ihling, G. M. Clore, A. Sinz, Mapping the toporogy and determination of a low-resolution three-dimensional structure of the calmodulin-melittin complex by chemical cross-linking and high-resolution FTICRMS: Direct demonstration of multiple binding modes, Biochem. 43, 4703-4715 (2004).
    • (2004) Biochem. , vol.43 , pp. 4703-4715
    • Schulz, D.M.1    Ihling, C.2    Clore, G.M.3    Sinz, A.4
  • 7
    • 0035810504 scopus 로고    scopus 로고
    • Conformation changes, complexation, and phase transition in matrix-assisted laser desorption
    • M. Sadeghi, X. Wu, A. Vertes, Conformation changes, complexation, and phase transition in matrix-assisted laser desorption, J. Phys. Chem. B, 105, 2578-2587 (2001).
    • (2001) J. Phys. Chem. B , vol.105 , pp. 2578-2587
    • Sadeghi, M.1    Wu, X.2    Vertes, A.3
  • 12
    • 85162647822 scopus 로고
    • A review of information theory in analytical chemometrics
    • K. Eckschlager, V. Stepanek, K. Danzer, A review of information theory in analytical chemometrics, J Chemometrics 4, 195-216 (1990).
    • (1990) J Chemometrics , vol.4 , pp. 195-216
    • Eckschlager, K.1    Stepanek, V.2    Danzer, K.3
  • 13
    • 0022543912 scopus 로고
    • High performance liquid chromatography and time-of-flight secondary ion mass spectrometry: A new dimension in structural analysis of apolipoproteins
    • H. U. Jabs, G. Assmann, D. Greifendorf, A. Benninghoven, High performance liquid chromatography and time-of-flight secondary ion mass spectrometry: A new dimension in structural analysis of apolipoproteins, J. Lipid Res. 27, 613-621 (1986).
    • (1986) J. Lipid Res. , vol.27 , pp. 613-621
    • Jabs, H.U.1    Assmann, G.2    Greifendorf, D.3    Benninghoven, A.4
  • 14
    • 0027917389 scopus 로고
    • Static secondary ion mass spectrometry of adsorbed proteins
    • D. S. Mantus, B. D. Ratner, B. A. Carlson, J. F. Moulder, Static secondary ion mass spectrometry of adsorbed proteins, Anal. Chem. 65(10), 1431-1438 (1993).
    • (1993) Anal. Chem. , vol.65 , Issue.10 , pp. 1431-1438
    • Mantus, D.S.1    Ratner, B.D.2    Carlson, B.A.3    Moulder, J.F.4
  • 15
    • 0029985914 scopus 로고    scopus 로고
    • A correlative study of the measurement of protein adsorption to steel, glass, polypropylene, and silicone surfaces using ToF-SIMS and dynamic contact angle analyses
    • J. Davies, C. S. Nunnerley, A. J. Paul, A correlative study of the measurement of protein adsorption to steel, glass, polypropylene, and silicone surfaces using ToF-SIMS and dynamic contact angle analyses, Colloid. Surf. B 6, 181-190 (1996).
    • (1996) Colloid. Surf. B , vol.6 , pp. 181-190
    • Davies, J.1    Nunnerley, C.S.2    Paul, A.J.3
  • 16
    • 0036692810 scopus 로고    scopus 로고
    • Role of salts on the BSA adsorption on stainless steel in aqueous solutions. II. ToF-SIMS spectral and chemical mapping study
    • C. Poleunis, C. Rubio, C. Compére, P. Bertrand, Role of salts on the BSA adsorption on stainless steel in aqueous solutions. II. ToF-SIMS spectral and chemical mapping study, Surf. Interf. Anal. 34, 55-58 (2002).
    • (2002) Surf. Interf. Anal. , vol.34 , pp. 55-58
    • Poleunis, C.1    Rubio, C.2    Compére, C.3    Bertrand, P.4
  • 17
    • 0038636988 scopus 로고    scopus 로고
    • Orientation modulation of a synthetic polypeptide in self-assembled monolayers: A TOF-SIMS study
    • K. Leufgen, M. Mutter, H. Vogel, W. Szymczak, Orientation modulation of a synthetic polypeptide in self-assembled monolayers: A TOF-SIMS study, J. Am. chem. Soc. 125, 8911-8915 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8911-8915
    • Leufgen, K.1    Mutter, M.2    Vogel, H.3    Szymczak, W.4
  • 18
    • 0038462129 scopus 로고    scopus 로고
    • Time-of-flight secondary ion mass spectrometry: Techniques and applications for the characterization of biomaterial surfaces
    • A. M. Belu, D. J. Graham, D. G Castner, Time-of-flight secondary ion mass spectrometry: Techniques and applications for the characterization of biomaterial surfaces, Biomaterials 24, 3635-3653 (2003).
    • (2003) Biomaterials , vol.24 , pp. 3635-3653
    • Belu, A.M.1    Graham, D.J.2    Castner, D.G.3
  • 20
    • 0035943196 scopus 로고    scopus 로고
    • Characterization of adsorbed protein films by time-of-flight secondary ion mass spectrometry with principal component analysis
    • M. S. Wagner, D. G. Castner, Characterization of adsorbed protein films by time-of-flight secondary ion mass spectrometry with principal component analysis, Langmuir 17, 4649-4660 (2001).
    • (2001) Langmuir , vol.17 , pp. 4649-4660
    • Wagner, M.S.1    Castner, D.G.2
  • 21
    • 0345600993 scopus 로고    scopus 로고
    • Preserving the structure of adsorbed protein films for time-of-flight secondary ion mass spectrometry analysis
    • N. Xia, D. G. Castner, Preserving the structure of adsorbed protein films for time-of-flight secondary ion mass spectrometry analysis, J. Biomed. Mater. Res. 67A, 179-190 (2003).
    • (2003) J. Biomed. Mater. Res. , vol.67 A , pp. 179-190
    • Xia, N.1    Castner, D.G.2
  • 22
    • 1542345315 scopus 로고    scopus 로고
    • Probing the orientation of surface-immobilized immunoglobulin G by time-of-flight secondary ion mass spectrometry
    • H. Wang, D. G. Castner, B. D. Ratner, S. Jiang, Probing the orientation of surface-immobilized immunoglobulin G by time-of-flight secondary ion mass spectrometry, Lagmuir 20, 1877-1887 (2004).
    • (2004) Lagmuir , vol.20 , pp. 1877-1887
    • Wang, H.1    Castner, D.G.2    Ratner, B.D.3    Jiang, S.4
  • 23
    • 0035420140 scopus 로고    scopus 로고
    • Bioengineered material surfaces for medical applications
    • H. J. Mathieu, Bioengineered material surfaces for medical applications, Surf. Interf. Anal. 32, 3-9 (2001).
    • (2001) Surf. Interf. Anal. , vol.32 , pp. 3-9
    • Mathieu, H.J.1
  • 24
    • 2342581561 scopus 로고    scopus 로고
    • Estimation of protein adsorption on dialysis membrane by means of TOF-SIMS imaging
    • S. Aoyagi, M. Hayama, U. Hasegawa, K. Sakai, M. Tozu, T. Hoshi, M. Kudo, Estimation of protein adsorption on dialysis membrane by means of TOF-SIMS imaging, J. Membr. Sci. 236(1-2), 91-99 (2004).
    • (2004) J. Membr. Sci. , vol.236 , Issue.1-2 , pp. 91-99
    • Aoyagi, S.1    Hayama, M.2    Hasegawa, U.3    Sakai, K.4    Tozu, M.5    Hoshi, T.6    Kudo, M.7
  • 25
    • 33748266733 scopus 로고    scopus 로고
    • Mutual information theory for biomedical applications
    • in press
    • S. Aoyagi and M. Kudo, Mutual Information Theory for Biomedical Applications, Appl. Surf. Sci., (in press).
    • Appl. Surf. Sci.
    • Aoyagi, S.1    Kudo, M.2
  • 26
    • 2942586972 scopus 로고    scopus 로고
    • TOF-SIMS investigation of metallic material surface after culturing cells
    • S. Aoyagi, S. Hiromoto, T. Hanawa, M. Kudo, TOF-SIMS investigation of metallic material surface after culturing cells, Appl. Surf. Sci. 231-232, 470-474 (2004).
    • (2004) Appl. Surf. Sci. , vol.231-232 , pp. 470-474
    • Aoyagi, S.1    Hiromoto, S.2    Hanawa, T.3    Kudo, M.4
  • 27
    • 14844325834 scopus 로고    scopus 로고
    • Surface characterization of the extracellular matrix remaining after cell, detachment from a thermoresponsive polymer
    • H. E. Canavan, X. H. Cheng, D. J. Graham, B. D. Ratner, D. G. Castner, Surface characterization of the extracellular matrix remaining after cell, detachment from a thermoresponsive polymer, Langmuir 21(5), 1949-1955 (2005).
    • (2005) Langmuir , vol.21 , Issue.5 , pp. 1949-1955
    • Canavan, H.E.1    Cheng, X.H.2    Graham, D.J.3    Ratner, B.D.4    Castner, D.G.5
  • 28
    • 33646859762 scopus 로고    scopus 로고
    • Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center
    • T. Waratrujiwong, B. Krebs, F. Spener, P. Visoottiviseth, Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center, FEBS J. 273(8), 1649-1659 (2006).
    • (2006) FEBS J. , vol.273 , Issue.8 , pp. 1649-1659
    • Waratrujiwong, T.1    Krebs, B.2    Spener, F.3    Visoottiviseth, P.4
  • 29
    • 25844449070 scopus 로고    scopus 로고
    • A new analysis of the depolymerized fragments of lignin polymer using ToF-SIMS
    • K. Saito, T. Kato, H. Takamori, T. Kishimoto, K. Fukushima, A new analysis of the depolymerized fragments of lignin polymer using ToF-SIMS, Biomacromol. 6(5), 2688-2696 (2005).
    • (2005) Biomacromol. , vol.6 , Issue.5 , pp. 2688-2696
    • Saito, K.1    Kato, T.2    Takamori, H.3    Kishimoto, T.4    Fukushima, K.5
  • 30
    • 18044385611 scopus 로고    scopus 로고
    • Surface morphology and chemistry of Prunus laurocerasus L. leaves: A study using X-ray photoelectron spectroscopy, time-of-flight secondary-ion mass spectrometry, atomic-force microscopy and scanning-electron microscopy
    • M. C. Perkins, C. J. Roberts, D. Briggs, M. C. Davies, A. Friedmann, C. A. Hart, G.A. Bell, Surface morphology and chemistry of Prunus laurocerasus L. leaves: a study using X-ray photoelectron spectroscopy, time-of-flight secondary-ion mass spectrometry, atomic-force microscopy and scanning-electron microscopy, Planta 221(1), 123-134 (2005).
    • (2005) Planta , vol.221 , Issue.1 , pp. 123-134
    • Perkins, M.C.1    Roberts, C.J.2    Briggs, D.3    Davies, M.C.4    Friedmann, A.5    Hart, C.A.6    Bell, G.A.7
  • 31
    • 11144239314 scopus 로고    scopus 로고
    • Effective monitoring of protein reaction on glass plate surfaces by TOF-SIMS
    • S. Aoyagi and M. Kudo, Effective monitoring of protein reaction on glass plate surfaces by TOF-SIMS, Biosens. Bioelectron. 20(8), 1626-1630 (2005).
    • (2005) Biosens. Bioelectron. , vol.20 , Issue.8 , pp. 1626-1630
    • Aoyagi, S.1    Kudo, M.2
  • 32
    • 3242772209 scopus 로고    scopus 로고
    • Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry
    • B. X. Huang, H. Y. Kim, C. Dass, Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry, J. Am. Soc. Mass Spectrom. 15(8), 1237-1247 (2004).
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , Issue.8 , pp. 1237-1247
    • Huang, B.X.1    Kim, H.Y.2    Dass, C.3
  • 33
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • S. Curry, H. Mandelkow, P. Brick, N. Franks, Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites, Nat. Struct. Biol. 5, 827-835 (1998).
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.