메뉴 건너뛰기




Volumn 337, Issue 2, 2005, Pages 294-307

Mass spectrometric analysis of affinity-captured proteins on a dendrimer-based immunosensing surface: Investigation of on-chip proteolytic digestion

Author keywords

Dendrimer monolayers; Immunosensing; MALDI TOF MS; On chip digestion; Peptide mass mapping

Indexed keywords

AMINO ACIDS; ANTIGEN-ANTIBODY REACTIONS; CHEMICAL DETECTION; DENDRIMERS; DESORPTION; EFFICIENCY; ESCHERICHIA COLI; MAMMALS; MASS SPECTROMETRY; MONOLAYERS; PEPTIDES;

EID: 13244275213     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.10.042     Document Type: Article
Times cited : (24)

References (45)
  • 1
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • S.P. Gygi, B. Rist, S.A. Gerber, F. Turecek, M.H. Gelb, and R. Aebersold Quantitative analysis of complex protein mixtures using isotope-coded affinity tags Nat. Biotechnol. 17 1999 994 999
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 3
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • B. Blagoev, I. Kratchmarova, S.E. Ong, M. Nielsen, L.J. Foster, and M. Mann A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling Nat. Biotechnol. 21 2003 315 318
    • (2003) Nat. Biotechnol. , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 4
    • 0002841275 scopus 로고    scopus 로고
    • BIA-MS-MS: Biomolecular interaction analysis for functional proteomics
    • T. Natsume, H. Nakayame, and T. Isobe BIA-MS-MS: biomolecular interaction analysis for functional proteomics Trends Biotechnol. 19 Suppl 2001 S28 S33
    • (2001) Trends Biotechnol. , vol.19 , Issue.SUPPL.
    • Natsume, T.1    Nakayame, H.2    Isobe, T.3
  • 6
    • 0037289438 scopus 로고    scopus 로고
    • High affinity capture surface for matrix-assisted laser desorption/ionisation compatible protein microarrays
    • J.O. Koopmann, and J. Blackburn High affinity capture surface for matrix-assisted laser desorption/ionisation compatible protein microarrays Rapid Commun. Mass Spectrom. 17 2003 455 462
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 455-462
    • Koopmann, J.O.1    Blackburn, J.2
  • 7
    • 0242354926 scopus 로고    scopus 로고
    • Parallel determination of multiple protein metabolite interactions using cell extract, protein microarrays, and mass spectrometric detection
    • V.N. Morozov, T.Y. Morozova, K.L. Johnson, and S. Naylor Parallel determination of multiple protein metabolite interactions using cell extract, protein microarrays, and mass spectrometric detection Rapid Commun. Mass Spectrom. 17 2003 2430 2438
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 2430-2438
    • Morozov, V.N.1    Morozova, T.Y.2    Johnson, K.L.3    Naylor, S.4
  • 8
    • 10744225132 scopus 로고    scopus 로고
    • Chip-based analysis of protein-protein interactions by fluorescence detection and on-chip immunoprecipitation combined with μlC-MS/MS analysis
    • J.R. Sydor, M. Scalf, S. Sideris, G.D. Mao, Y. Pandey, M. Tan, M. Mariano, M.F. Moran, S. Nock, and P. Wagner Chip-based analysis of protein-protein interactions by fluorescence detection and on-chip immunoprecipitation combined with μLC-MS/MS analysis Anal. Chem. 75 2003 6163 6170
    • (2003) Anal. Chem. , vol.75 , pp. 6163-6170
    • Sydor, J.R.1    Scalf, M.2    Sideris, S.3    Mao, G.D.4    Pandey, Y.5    Tan, M.6    Mariano, M.7    Moran, M.F.8    Nock, S.9    Wagner, P.10
  • 9
    • 0036683495 scopus 로고    scopus 로고
    • Enhanced affinity capture MALDI-TOF MS: Orientation of an immunoglobulin G using recombinant protein G
    • H. Neubert, E.S. Jacoby, S.S. Bansal, R.K. Iles, D.A. Cowan, and A.T. Kicman Enhanced affinity capture MALDI-TOF MS: orientation of an immunoglobulin G using recombinant protein G Anal. Chem. 74 2002 3677 3683
    • (2002) Anal. Chem. , vol.74 , pp. 3677-3683
    • Neubert, H.1    Jacoby, E.S.2    Bansal, S.S.3    Iles, R.K.4    Cowan, D.A.5    Kicman, A.T.6
  • 10
    • 0034257917 scopus 로고    scopus 로고
    • Combination of biomolecular interaction analysis and mass spectrometric amino acid sequencing
    • T. Natsume, H. Nakayama, O. Jansson, T. Isobe, K. Takio, and K. Mikoshiba Combination of biomolecular interaction analysis and mass spectrometric amino acid sequencing Anal. Chem. 72 2000 4193 4198
    • (2000) Anal. Chem. , vol.72 , pp. 4193-4198
    • Natsume, T.1    Nakayama, H.2    Jansson, O.3    Isobe, T.4    Takio, K.5    Mikoshiba, K.6
  • 11
    • 0034666508 scopus 로고    scopus 로고
    • Multitoxin biosensor-mass spectrometry analysis: A new approach for rapid, real-time, sensitive analysis of staphylococcal toxins in food
    • D. Nedelkov, A. Rasooly, and R.W. Nelson Multitoxin biosensor-mass spectrometry analysis: a new approach for rapid, real-time, sensitive analysis of staphylococcal toxins in food Int. J. Food Microbiol. 60 2000 1 13
    • (2000) Int. J. Food Microbiol. , vol.60 , pp. 1-13
    • Nedelkov, D.1    Rasooly, A.2    Nelson, R.W.3
  • 12
    • 0032113285 scopus 로고    scopus 로고
    • Combining MALDI mass spectrometry and biomolecular interaction analysis using a biomolecular interaction analysis instrument
    • C.P. Sönksen, E. Nordhoff, Ö. Jansson, M. Malmqvist, and P. Roepstorff Combining MALDI mass spectrometry and biomolecular interaction analysis using a biomolecular interaction analysis instrument Anal. Chem. 70 1998 2731 2736
    • (1998) Anal. Chem. , vol.70 , pp. 2731-2736
    • Sönksen, C.P.1    Nordhoff, E.2    Jansson, Ö.3    Malmqvist, M.4    Roepstorff, P.5
  • 14
    • 0038385497 scopus 로고    scopus 로고
    • Affinity mass spectrometry-based approaches for the analysis of protein-protein interaction and complex mixtures of peptide-ligands
    • A.H. Rüdiger, M. Rüdiger, U.D. Carl, T. Chakraborty, P. Roepstorff, and J. Wehland Affinity mass spectrometry-based approaches for the analysis of protein-protein interaction and complex mixtures of peptide-ligands Anal. Biochem. 275 1999 162 170
    • (1999) Anal. Biochem. , vol.275 , pp. 162-170
    • Rüdiger, A.H.1    Rüdiger, M.2    Carl, U.D.3    Chakraborty, T.4    Roepstorff, P.5    Wehland, J.6
  • 15
    • 0029646014 scopus 로고
    • Probe-immobilized affinity chromatography/mass spectrometry
    • A.H. Brockman, and R. Orlando Probe-immobilized affinity chromatography/mass spectrometry Anal. Chem. 67 1995 4581 4585
    • (1995) Anal. Chem. , vol.67 , pp. 4581-4585
    • Brockman, A.H.1    Orlando, R.2
  • 16
    • 0000399445 scopus 로고
    • Direct analysis of affinity-bound analytes by MALDI/TOF MS
    • D.I. Papac, J. Hoyes, and K.B. Tomer Direct analysis of affinity-bound analytes by MALDI/TOF MS Anal. Chem. 66 1994 2609 2613
    • (1994) Anal. Chem. , vol.66 , pp. 2609-2613
    • Papac, D.I.1    Hoyes, J.2    Tomer, K.B.3
  • 17
    • 0033103799 scopus 로고    scopus 로고
    • Advances in surface plasmon resonance biomolecular interaction analysis mass spectrometry (BIA/MS)
    • R.W. Nelson, and J.R. Krone Advances in surface plasmon resonance biomolecular interaction analysis mass spectrometry (BIA/MS) J. Mol. Recognit. 12 1999 77 93
    • (1999) J. Mol. Recognit. , vol.12 , pp. 77-93
    • Nelson, R.W.1    Krone, J.R.2
  • 18
    • 0038771153 scopus 로고    scopus 로고
    • Surface plasmon resonance mass spectrometry: Recent progress and outlooks
    • D. Nedelkov, and R.W. Nelson Surface plasmon resonance mass spectrometry: recent progress and outlooks Trends Biotechnol. 21 2003 301 305
    • (2003) Trends Biotechnol. , vol.21 , pp. 301-305
    • Nedelkov, D.1    Nelson, R.W.2
  • 19
    • 0038070646 scopus 로고    scopus 로고
    • On-column digestion of proteins in aqueous-organic solvents
    • G.W. Slysz, and D.C. Schriemer On-column digestion of proteins in aqueous-organic solvents Rapid Commun. Mass Spectrom. 17 2003 1044 1050
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 1044-1050
    • Slysz, G.W.1    Schriemer, D.C.2
  • 20
    • 0035356739 scopus 로고    scopus 로고
    • Proteolysis in mixed organic-aqueous solvent systems: Applications for peptide mass mapping using mass spectrometry
    • W.K. Russell, Z.Y. Park, and D.H. Russell Proteolysis in mixed organic-aqueous solvent systems: applications for peptide mass mapping using mass spectrometry Anal. Chem. 73 2001 2682 2685
    • (2001) Anal. Chem. , vol.73 , pp. 2682-2685
    • Russell, W.K.1    Park, Z.Y.2    Russell, D.H.3
  • 21
    • 0034212611 scopus 로고    scopus 로고
    • Thermal denaturation: A useful technique in peptide mass mapping
    • Z.Y. Park, and D.H. Russell Thermal denaturation: a useful technique in peptide mass mapping Anal. Chem. 72 2000 2667 2670
    • (2000) Anal. Chem. , vol.72 , pp. 2667-2670
    • Park, Z.Y.1    Russell, D.H.2
  • 22
    • 0036874381 scopus 로고    scopus 로고
    • Microcolumn capture and digestion of proteins combined with mass spectrometry for protein identification
    • D. Craft, A. Doucette, and L. Li Microcolumn capture and digestion of proteins combined with mass spectrometry for protein identification J. Proteome Res. 1 2002 537 547
    • (2002) J. Proteome Res. , vol.1 , pp. 537-547
    • Craft, D.1    Doucette, A.2    Li, L.3
  • 23
    • 1842476304 scopus 로고    scopus 로고
    • Integration of on-line protein digestion, peptide separation, and protein identification using pepsin-coated photopolymerized sol-gel columns and capillary electrophoresis/mass spectrometry
    • M. Kato, K. Sakai-Kato, H. Jin, K. Kubota, H. Miyano, T. Toyo'oka, M.T. Dulay, and R.N. Zare Integration of on-line protein digestion, peptide separation, and protein identification using pepsin-coated photopolymerized sol-gel columns and capillary electrophoresis/mass spectrometry Anal. Chem. 76 2004 1896 1902
    • (2004) Anal. Chem. , vol.76 , pp. 1896-1902
    • Kato, M.1    Sakai-Kato, K.2    Jin, H.3    Kubota, K.4    Miyano, H.5    Toyo'Oka, T.6    Dulay, M.T.7    Zare, R.N.8
  • 24
    • 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
    • D.S. Peterson, T. Rohr, F. Svec, and J.M.J. Fréchet Enzymatic microreactor-on-a-chip: protein mapping using trypsin immobilized on porous polymer monoliths molded in channels of microfluidic devices Anal. Chem. 74 2002 4081 4088
    • (2002) Anal. Chem. , vol.74 , pp. 4081-4088
    • Peterson, D.S.1    Rohr, T.2    Svec, F.3    Fréchet, J.M.J.4
  • 25
    • 0033868723 scopus 로고    scopus 로고
    • Integration of immobilized trypsin bead beds for protein digestion within a microfluidic chip incorporating capillary electrophoresis separations and an electrospray mass spectrometry interface
    • C. Wang, R. Oleschuk, F. Ouchen, J.J. Li, P. Thibault, and D.J. Harrison Integration of immobilized trypsin bead beds for protein digestion within a microfluidic chip incorporating capillary electrophoresis separations and an electrospray mass spectrometry interface Rapid Commun. Mass Spectrom. 14 2000 1377 1383
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1377-1383
    • Wang, C.1    Oleschuk, R.2    Ouchen, F.3    Li, J.J.4    Thibault, P.5    Harrison, D.J.6
  • 26
    • 0037457866 scopus 로고    scopus 로고
    • Protein-ligand interactions at poly (amidoamine) dendrimer monolayers on gold
    • M.Y. Hong, H.C. Yoon, and H.S. Kim Protein-ligand interactions at poly (amidoamine) dendrimer monolayers on gold Langmuir 19 2003 416 421
    • (2003) Langmuir , vol.19 , pp. 416-421
    • Hong, M.Y.1    Yoon, H.C.2    Kim, H.S.3
  • 28
    • 0043125601 scopus 로고    scopus 로고
    • Next generation of protein microarray support materials: Evaluation for protein and antibody microarray applications
    • P. Angenendt, J. Glökler, J. Sobek, H. Lehrach, and D.J. Cahill Next generation of protein microarray support materials: evaluation for protein and antibody microarray applications J. Chromatogr. A 1009 2003 97 104
    • (2003) J. Chromatogr. a , vol.1009 , pp. 97-104
    • Angenendt, P.1    Glökler, J.2    Sobek, J.3    Lehrach, H.4    Cahill, D.J.5
  • 30
    • 0036677307 scopus 로고    scopus 로고
    • Biocatalytic precipitation induced by an affinity reaction on dendrimer-activated surfaces for the electrochemical signaling from immunosensors
    • H.C. Yoon, H. Yang, and Y.T. Kim Biocatalytic precipitation induced by an affinity reaction on dendrimer-activated surfaces for the electrochemical signaling from immunosensors Analyst 127 2002 1082 1087
    • (2002) Analyst , vol.127 , pp. 1082-1087
    • Yoon, H.C.1    Yang, H.2    Kim, Y.T.3
  • 33
    • 0032513719 scopus 로고    scopus 로고
    • Preparation and characterization of dendrimer monolayers and dendrimer-alkanethiol mixed monolayers adsorbed to gold
    • H. Tokuhisa, M.Q. Zhao, L.A. Baker, V.T. Phan, D.L. Dermody, M.E. Garcia, and R.F. Peez Preparation and characterization of dendrimer monolayers and dendrimer-alkanethiol mixed monolayers adsorbed to gold J. Am. Chem. Soc. 120 1998 4492 4501
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4492-4501
    • Tokuhisa, H.1    Zhao, M.Q.2    Baker, L.A.3    Phan, V.T.4    Dermody, D.L.5    Garcia, M.E.6    Peez, R.F.7
  • 36
    • 0035253703 scopus 로고    scopus 로고
    • A quantitative assessment of heterogeneity for surface-immobilized proteins
    • R.A. Vijayendran, and D.E. Leckband A quantitative assessment of heterogeneity for surface-immobilized proteins Anal. Chem. 73 2001 471 480
    • (2001) Anal. Chem. , vol.73 , pp. 471-480
    • Vijayendran, R.A.1    Leckband, D.E.2
  • 37
    • 0029915191 scopus 로고    scopus 로고
    • Oriented immobilization of antibodies and its applications in immunoassays and immunosensors
    • B. Lu, M.R. Smyth, and R. O'Kennedy Oriented immobilization of antibodies and its applications in immunoassays and immunosensors Analyst 121 1996 R29 R32
    • (1996) Analyst , vol.121
    • Lu, B.1    Smyth, M.R.2    O'Kennedy, R.3
  • 38
    • 0031003589 scopus 로고    scopus 로고
    • Effectiveness of protein a for antibody immobilization for a fiber optic biosensor
    • G.P. Anderson, M.A. Jacoby, F.S. Ligler, and K.D. King Effectiveness of protein A for antibody immobilization for a fiber optic biosensor Biosens. Bioelectron. 12 1997 329 336
    • (1997) Biosens. Bioelectron. , vol.12 , pp. 329-336
    • Anderson, G.P.1    Jacoby, M.A.2    Ligler, F.S.3    King, K.D.4
  • 39
    • 0026153423 scopus 로고
    • Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins
    • E. Stenberg, B. Persson, H. Roos, and C. Urbaniczky Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins J. Colloid Interface Sci. 143 1991 513 526
    • (1991) J. Colloid Interface Sci. , vol.143 , pp. 513-526
    • Stenberg, E.1    Persson, B.2    Roos, H.3    Urbaniczky, C.4
  • 41
    • 5244278723 scopus 로고    scopus 로고
    • Site-specific immobilization of monoclonal antibodies using spacer-mediated antibody attachment
    • S.C. Huang, K.D. Caldwell, J.N. Lin, H.K. Wang, and J.N. Herron Site-specific immobilization of monoclonal antibodies using spacer-mediated antibody attachment Langmuir 12 1996 4292 4298
    • (1996) Langmuir , vol.12 , pp. 4292-4298
    • Huang, S.C.1    Caldwell, K.D.2    Lin, J.N.3    Wang, H.K.4    Herron, J.N.5
  • 42
    • 0025054642 scopus 로고
    • Binding of a monoclonal antibody and its Fab fragment to supported phospholipid monolayers measured by total internal reflection fluorescence microscopy
    • M.L. Pisarchick, and N.L. Thompson Binding of a monoclonal antibody and its Fab fragment to supported phospholipid monolayers measured by total internal reflection fluorescence microscopy Biophys. J. 58 1990 1235 1249
    • (1990) Biophys. J. , vol.58 , pp. 1235-1249
    • Pisarchick, M.L.1    Thompson, N.L.2
  • 43
    • 0036917313 scopus 로고    scopus 로고
    • Chips for proteomics: A new tool or just hype?
    • P. James Chips for proteomics: a new tool or just hype? BioTechniques 33 Suppl 2002 S4 S13
    • (2002) BioTechniques , vol.33 , Issue.SUPPL.
    • James, P.1
  • 45
    • 0032576977 scopus 로고    scopus 로고
    • Bactericidal domain of lactoferrin: Detection, quantitation, and characterization of lactoferricin in serum by SELDI affinity mass spectrometry
    • H. Kuwata, T.T. Yip, C.L. Yip, M. Tomita, and T.W. Hutchens Bactericidal domain of lactoferrin: detection, quantitation, and characterization of lactoferricin in serum by SELDI affinity mass spectrometry Biochem. Biophys. Res. Commun. 245 1998 764 773
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 764-773
    • Kuwata, H.1    Yip, T.T.2    Yip, C.L.3    Tomita, M.4    Hutchens, T.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.