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Volumn 310, Issue 2, 2002, Pages 137-147

Sequencing of rat liver cytosolic proteins by matrix-assisted laser desorption ionization - Quadrupole time-of-flight mass spectrometry following electrophoretic separation and extraction

Author keywords

Gel electrophoresis; MALDI QqTOF mass spectrometry; Posttranslational modification; Protein sequence analysis; Rat liver cytosolic proteins

Indexed keywords

AMINO ACIDS; DESORPTION; ELECTROPHORESIS; IONIZATION; PROTEINS; RATS; SOLVENT EXTRACTION;

EID: 1842865976     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(02)00321-4     Document Type: Article
Times cited : (13)

References (48)
  • 1
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • M. Wilm, A. Shevchenko, T. Houthaeve, S. Breit, L. Schweigerer, T. Fotsis, M. Mann, Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry, Nature 379 (1996) 466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 3
    • 0031962612 scopus 로고    scopus 로고
    • Mass spectrometry and the age of the proteome
    • J.R. Yates, Mass spectrometry and the age of the proteome, J. Mass Spectrom. 33 (1998) 1-19.
    • (1998) J. Mass Spectrom. , vol.33 , pp. 1-19
    • Yates, J.R.1
  • 5
    • 0033230904 scopus 로고    scopus 로고
    • Toward a clinical molecular scanner for proteome research: Parallel protein chemical processing before and during Western blot
    • W.V. Bienvenut, J.C. Sanchez, A. Karmime, V. Rouge, K. Rose, P.A. Binz, D.F. Hochstrasser, Toward a clinical molecular scanner for proteome research: parallel protein chemical processing before and during Western blot, Anal. Chem. 71 (1999) 4800-4807.
    • (1999) Anal. Chem. , vol.71 , pp. 4800-4807
    • Bienvenut, W.V.1    Sanchez, J.C.2    Karmime, A.3    Rouge, V.4    Rose, K.5    Binz, P.A.6    Hochstrasser, D.F.7
  • 7
    • 0034654593 scopus 로고    scopus 로고
    • Site-specific mass tagging with stable isotopes in proteins for accurate and efficient protein identification
    • X. Chen, L.M. Smith, E.M. Bradbury, Site-specific mass tagging with stable isotopes in proteins for accurate and efficient protein identification, Anal. Chem. 72 (2000) 1134-1143.
    • (2000) Anal. Chem. , vol.72 , pp. 1134-1143
    • Chen, X.1    Smith, L.M.2    Bradbury, E.M.3
  • 8
    • 0034234766 scopus 로고    scopus 로고
    • Improvements in protein identification by MALDI-TOF-MS peptide mapping
    • V. Egelhofer, K. Bussow, C. Luebbert, H. Lehrach, E. Nordhoff, Improvements in protein identification by MALDI-TOF-MS peptide mapping, Anal. Chem. 72 (2000) 2741-2750.
    • (2000) Anal. Chem. , vol.72 , pp. 2741-2750
    • Egelhofer, V.1    Bussow, K.2    Luebbert, C.3    Lehrach, H.4    Nordhoff, E.5
  • 10
    • 0028824080 scopus 로고
    • Mass spectrometric approaches for the identification of gel-separated proteins
    • S.D. Patterson, R. Aebersold, Mass spectrometric approaches for the identification of gel-separated proteins, Electrophoresis 16 (1995) 1791-1814.
    • (1995) Electrophoresis , vol.16 , pp. 1791-1814
    • Patterson, S.D.1    Aebersold, R.2
  • 11
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins in silver-stained polyacrylamide gels
    • A. Shevchenko, M. Wilm, O. Vorm, M. Mann, Mass spectrometric sequencing of proteins in silver-stained polyacrylamide gels, Anal. Chem. 68 (1996) 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 12
    • 0034194446 scopus 로고    scopus 로고
    • MALDI quadrupole time-of-flight mass spectrometry: A powerful tool for proteomic research
    • A. Shevchenko, A. Loboda, W. Ens, K.G. Standing, MALDI quadrupole time-of-flight mass spectrometry: a powerful tool for proteomic research, Anal. Chem. 72 (2000) 2132-2141.
    • (2000) Anal. Chem. , vol.72 , pp. 2132-2141
    • Shevchenko, A.1    Loboda, A.2    Ens, W.3    Standing, K.G.4
  • 14
    • 0031568420 scopus 로고    scopus 로고
    • Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level
    • A.L. McCormack, D.M. Schieltz, B. Goode, S. Yang, G. Barnes, D. Drubin, J.R. Yates III, Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level, Anal. Chem. 69 (1997) 767-776.
    • (1997) Anal. Chem. , vol.69 , pp. 767-776
    • McCormack, A.L.1    Schieltz, D.M.2    Goode, B.3    Yang, S.4    Barnes, G.5    Drubin, D.6    Yates J.R. III7
  • 15
    • 0032535467 scopus 로고    scopus 로고
    • Modification of cysteine residues by alkylation, a tool in peptide mapping and protein identification
    • S. Sechi, B.T. Chait, Modification of cysteine residues by alkylation, a tool in peptide mapping and protein identification, Anal. Chem. 70 (1998) 5150-5158.
    • (1998) Anal. Chem. , vol.70 , pp. 5150-5158
    • Sechi, S.1    Chait, B.T.2
  • 17
    • 0033594994 scopus 로고    scopus 로고
    • A method for high-sensitivity peptide sequencing using postsource decay matrix-assisted laser desorption ionization mass spectrometry
    • T. Keough, R.S. Youngquist, M.P. Lacey, A method for high-sensitivity peptide sequencing using postsource decay matrix-assisted laser desorption ionization mass spectrometry, Proc. Natl. Acad. Sci. USA 96 (1999) 7131-7136.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7131-7136
    • Keough, T.1    Youngquist, R.S.2    Lacey, M.P.3
  • 18
    • 0034120963 scopus 로고    scopus 로고
    • Sequencing of sulfonic acid derivatized peptides by electrospray mass spectrometry
    • M.D. Bauer, Y. Sun, T. Keough, M.P. Lacey, Sequencing of sulfonic acid derivatized peptides by electrospray mass spectrometry, Rapid Commun. Mass Spectrom. 14 (2000) 924-929.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 924-929
    • Bauer, M.D.1    Sun, Y.2    Keough, T.3    Lacey, M.P.4
  • 19
    • 0030960366 scopus 로고    scopus 로고
    • Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer
    • A. Shevchenko, I. Chernushevich, W. Ens, K.G. Standing, B. Thomson, M. Wilm, M. Mann, Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer, Rapid Commun. Mass Spectrom. 11 (1997) 1015-1024.
    • (1997) Rapid Commun. Mass Spectrom. , vol.11 , pp. 1015-1024
    • Shevchenko, A.1    Chernushevich, I.2    Ens, W.3    Standing, K.G.4    Thomson, B.5    Wilm, M.6    Mann, M.7
  • 20
    • 0033106490 scopus 로고    scopus 로고
    • 18O-labeling of N-glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching
    • 18O-labeling of N-glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching, Anal. Chem. 71 (1999) 1431-1440.
    • (1999) Anal. Chem. , vol.71 , pp. 1431-1440
    • Kuster, B.1    Mann, M.2
  • 21
    • 0034282457 scopus 로고    scopus 로고
    • Quantitation and facilitated de novo sequencing of proteins by isotopic N-terminal labeling of peptides with a fragmentation-directing moiety
    • M. Munchbach, M. Quadroni, G. Miotto, P. James, Quantitation and facilitated de novo sequencing of proteins by isotopic N-terminal labeling of peptides with a fragmentation-directing moiety, Anal. Chem. 72 (2000) 4047-4057.
    • (2000) Anal. Chem. , vol.72 , pp. 4047-4057
    • Munchbach, M.1    Quadroni, M.2    Miotto, G.3    James, P.4
  • 22
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • K.R. Clauser, P. Baker, A.L. Burlingame, Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching, Anal. Chem. 71 (1999) 2871-2882.
    • (1999) Anal. Chem. , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 23
    • 0034653646 scopus 로고    scopus 로고
    • Protein identification with a single accurate mass of a cysteine-containing peptide and constrained database searching
    • D.R. Goodlett, J.E. Bruce, G.A. Anderson, B. Rist, L. Pasa-Tolic, O. Fiehn, R.D. Smith, R. Aebersold, Protein identification with a single accurate mass of a cysteine-containing peptide and constrained database searching, Anal. Chem. 72 (2000) 1112-1118.
    • (2000) Anal. Chem. , vol.72 , pp. 1112-1118
    • Goodlett, D.R.1    Bruce, J.E.2    Anderson, G.A.3    Rist, B.4    Pasa-Tolic, L.5    Fiehn, O.6    Smith, R.D.7    Aebersold, R.8
  • 24
    • 0035866680 scopus 로고    scopus 로고
    • High-mass accuracy of product ions produced by SORI-CID using a dual electrospray ionization source coupled with FTICR mass spectrometry
    • J.W. Flora, J.C. Hannis, D.C. Muddiman, High-mass accuracy of product ions produced by SORI-CID using a dual electrospray ionization source coupled with FTICR mass spectrometry, Anal. Chem. 73 (2001) 1247-1251.
    • (2001) Anal. Chem. , vol.73 , pp. 1247-1251
    • Flora, J.W.1    Hannis, J.C.2    Muddiman, D.C.3
  • 25
    • 0034124238 scopus 로고    scopus 로고
    • A tandem quadrupole/time-of-flight mass spectrometer with a matrix-assisted laser desorption/ionization source: Design and performance
    • A.V. Loboda, A.N. Krutchinsky, M. Bromirski, W. Ens, K.G. Standing, A tandem quadrupole/time-of-flight mass spectrometer with a matrix-assisted laser desorption/ionization source: design and performance, Rapid Commun. Mass Spectrom. 14 (2000) 1047-1057.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1047-1057
    • Loboda, A.V.1    Krutchinsky, A.N.2    Bromirski, M.3    Ens, W.4    Standing, K.G.5
  • 26
  • 27
    • 0033429309 scopus 로고    scopus 로고
    • Electrospray mass spectra from protein electroeluted from sodium dodecylsulfate polyacrylamide gel electrophoresis gels
    • E.K. Fridriksson, B. Baird, F.W. McLafferty, Electrospray mass spectra from protein electroeluted from sodium dodecylsulfate polyacrylamide gel electrophoresis gels, J. Am. Soc. Mass Spectrom. 10 (1999) 453-455.
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 453-455
    • Fridriksson, E.K.1    Baird, B.2    McLafferty, F.W.3
  • 28
    • 0031148680 scopus 로고    scopus 로고
    • Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels
    • S.L. Cohen, B.T. Chait, Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels, Anal. Biochem. 247 (1997) 257-267.
    • (1997) Anal. Biochem. , vol.247 , pp. 257-267
    • Cohen, S.L.1    Chait, B.T.2
  • 29
    • 0034282758 scopus 로고    scopus 로고
    • Peptide electroextraction for direct coupling of in-gel digests with capillary LC-MS/MS for protein identification and sequencing
    • A.T. Timperman, R. Aebersold, Peptide electroextraction for direct coupling of in-gel digests with capillary LC-MS/MS for protein identification and sequencing, Anal. Chem. 72 (2000) 4115-4121.
    • (2000) Anal. Chem. , vol.72 , pp. 4115-4121
    • Timperman, A.T.1    Aebersold, R.2
  • 30
    • 0022090989 scopus 로고
    • The recovery of nitrocellulose-bound protein
    • P.J. Anderson, The recovery of nitrocellulose-bound protein, Anal. Biochem. 148 (1985) 105-110.
    • (1985) Anal. Biochem. , vol.148 , pp. 105-110
    • Anderson, P.J.1
  • 31
    • 0027472843 scopus 로고
    • Optimization of sample recovery from the nitrocellulose support used in plasma desorption mass spectrometry and its use for multiple analyses of insulin
    • S. Jespersen, G. Talbo, P. Roepstorff, Optimization of sample recovery from the nitrocellulose support used in plasma desorption mass spectrometry and its use for multiple analyses of insulin, Biol. Mass Spectrom. 22 (1993) 77-83.
    • (1993) Biol. Mass Spectrom. , vol.22 , pp. 77-83
    • Jespersen, S.1    Talbo, G.2    Roepstorff, P.3
  • 32
    • 0030588172 scopus 로고    scopus 로고
    • Methodical analysis of protein-nitrocellulose interactions to design a refined digestion protocol
    • M. Lui, P. Tempst, H. Erdjument-Bromage, Methodical analysis of protein-nitrocellulose interactions to design a refined digestion protocol, Anal. Biochem. 241 (1996) 156-166.
    • (1996) Anal. Biochem. , vol.241 , pp. 156-166
    • Lui, M.1    Tempst, P.2    Erdjument-Bromage, H.3
  • 33
    • 0023430927 scopus 로고
    • Internal amino acid sequence analysis of proteins separated by one- or two-dimensional gel electrophoresis after in situ protease digestion on nitrocellulose
    • R.H. Aebersold, J. Leavitt, R.A. Saavedra, L.E. Hood, S.B. Kent, Internal amino acid sequence analysis of proteins separated by one- or two-dimensional gel electrophoresis after in situ protease digestion on nitrocellulose, Proc. Natl. Acad. Sci. USA 84 (1987) 6970-6974.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6970-6974
    • Aebersold, R.H.1    Leavitt, J.2    Saavedra, R.A.3    Hood, L.E.4    Kent, S.B.5
  • 35
    • 0027656441 scopus 로고
    • Reproducibility and quantitation of matrix-assisted laser desorption ionization mass spectrometry: Effects of nitrocellulose on peptide ion yields
    • L.M. Preston, K.K. Murray, D.H. Russell, Reproducibility and quantitation of matrix-assisted laser desorption ionization mass spectrometry: effects of nitrocellulose on peptide ion yields, Biol. Mass Spectrom. 22 (1993) 544-550.
    • (1993) Biol. Mass Spectrom. , vol.22 , pp. 544-550
    • Preston, L.M.1    Murray, K.K.2    Russell, D.H.3
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 39
    • 0033169004 scopus 로고    scopus 로고
    • Orthogonal-injection time-of-fight mass spectrometry for analysis of biomolecules
    • I.V. Chernushevich, W. Ens, K.G. Standing, Orthogonal-injection time-of-fight mass spectrometry for analysis of biomolecules, Anal. Chem. 71 (1999) 452A-461A.
    • (1999) Anal. Chem. , vol.71
    • Chernushevich, I.V.1    Ens, W.2    Standing, K.G.3
  • 41
    • 0035827565 scopus 로고    scopus 로고
    • Determination of the complete amino acid sequence for the coat protein of brome mosaic virus by time-of-flight mass spectrometry: Evidence for mutations associated with change of propagation host
    • Y.M. She, S. Haber, D.L. Seifers, A. Lobada, I. Chernushevich, H. Perreault, W. Ens, K.G. Standing, Determination of the complete amino acid sequence for the coat protein of brome mosaic virus by time-of-flight mass spectrometry: evidence for mutations associated with change of propagation host, J. Biol. Chem. 276 (2001) 20039-20047.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20039-20047
    • She, Y.M.1    Haber, S.2    Seifers, D.L.3    Lobada, A.4    Chernushevich, I.5    Perreault, H.6    Ens, W.7    Standing, K.G.8
  • 42
    • 12044260066 scopus 로고
    • Matrix-assisted laser desorption ionization mass spectrometry of proteins electroblotted after polyacrylamide gel electrophoresis
    • K. Strupat, M. Karas, F. Hillenkamp, C. Eckerskorn, F. Lottspeich, Matrix-assisted laser desorption ionization mass spectrometry of proteins electroblotted after polyacrylamide gel electrophoresis, Anal. Chem. 66 (1994) 464-470.
    • (1994) Anal. Chem. , vol.66 , pp. 464-470
    • Strupat, K.1    Karas, M.2    Hillenkamp, F.3    Eckerskorn, C.4    Lottspeich, F.5
  • 43
    • 0030584491 scopus 로고    scopus 로고
    • Characterization of SDS-PAGE separated proteins by matrix-assisted laser desorption/ionization mass spectrometry
    • X. Liang, J. Bai, Y.H. Liu, D.M. Lubman, Characterization of SDS-PAGE separated proteins by matrix-assisted laser desorption/ionization mass spectrometry, Anal. Chem. 68 (1996) 1012-1018.
    • (1996) Anal. Chem. , vol.68 , pp. 1012-1018
    • Liang, X.1    Bai, J.2    Liu, Y.H.3    Lubman, D.M.4
  • 44
    • 0031241394 scopus 로고    scopus 로고
    • Identification and characterization of post-translational modifications of proteins by MALDI ion trap mass spectrometry
    • J. Qin, B.T. Chait, Identification and characterization of post-translational modifications of proteins by MALDI ion trap mass spectrometry, Anal. Chem. 69 (1997) 4002-4009.
    • (1997) Anal. Chem. , vol.69 , pp. 4002-4009
    • Qin, J.1    Chait, B.T.2
  • 45
    • 0023664899 scopus 로고
    • cDNA and deduced amino acid sequence of rat copper-zinc-containing superoxide dismutase
    • Y.S. Ho, J.D. Crapo, cDNA and deduced amino acid sequence of rat copper-zinc-containing superoxide dismutase, Nucleic Acids Res. 15 (1987) 6746.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 6746
    • Ho, Y.S.1    Crapo, J.D.2
  • 46
    • 0025057082 scopus 로고
    • Glutathione-protein mixed disulfide decreases the affinity of rat liver fatty acid-binding protein for unsaturated fatty acid
    • M. Hitomi, S. Odani, T. Ono, Glutathione-protein mixed disulfide decreases the affinity of rat liver fatty acid-binding protein for unsaturated fatty acid, Eur. J. Biochem. 187 (1990) 713-719.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 713-719
    • Hitomi, M.1    Odani, S.2    Ono, T.3
  • 47
    • 0027166062 scopus 로고
    • Amino acid exchange and covalent modification by cysteine and glutathione explain isoforms of fatty acid-binding protein occurring in bovine liver
    • P. Dörmann, T. Börchers, U. Korf, P. Højrup, P. Roepstorff, F. Spener, Amino acid exchange and covalent modification by cysteine and glutathione explain isoforms of fatty acid-binding protein occurring in bovine liver, J. Biol. Chem. 268 (1993) 16286-16292.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16286-16292
    • Dörmann, P.1    Börchers, T.2    Korf, U.3    Højrup, P.4    Roepstorff, P.5    Spener, F.6
  • 48
    • 0033521690 scopus 로고    scopus 로고
    • Isolation and characterization of two distinct forms of liver fatty acid binding protein from the rat
    • E.J. Murphy, R.D. Edmondson, D.H. Russell, S. Colles, F. Schroeder, Isolation and characterization of two distinct forms of liver fatty acid binding protein from the rat, Biochim. Biophys. Acta 1436 (1999) 413-425.
    • (1999) Biochim. Biophys. Acta , vol.1436 , pp. 413-425
    • Murphy, E.J.1    Edmondson, R.D.2    Russell, D.H.3    Colles, S.4    Schroeder, F.5


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