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Volumn 383, Issue 2, 2008, Pages 137-143

Previsible silver staining of protein in electrophoresis gels with mass spectrometry compatibility

Author keywords

Ethyl violet; MALDI MS; Previsible silver staining; Proteomics; Zincon

Indexed keywords

ELECTROPHORESIS; GELS; MASS SPECTROMETRY; METAL IONS; PROTEINS; PROTEOMICS; SODIUM DODECYL SULFATE; SULFUR COMPOUNDS;

EID: 54249117141     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.04.048     Document Type: Article
Times cited : (13)

References (31)
  • 1
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell P.H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250 (1975) 4007-4021
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 3
    • 0037023859 scopus 로고    scopus 로고
    • Detection technologies in proteome analysis
    • Patton W.F. Detection technologies in proteome analysis. J. Chromatogr. B 771 (2002) 3-31
    • (2002) J. Chromatogr. B , vol.771 , pp. 3-31
    • Patton, W.F.1
  • 4
    • 3042665732 scopus 로고    scopus 로고
    • Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis
    • Candiano G., Bruschi M., Musante L., and Santucci L. Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis. Electrophoresis 25 (2004) 1327-1333
    • (2004) Electrophoresis , vol.25 , pp. 1327-1333
    • Candiano, G.1    Bruschi, M.2    Musante, L.3    Santucci, L.4
  • 5
    • 0030273626 scopus 로고    scopus 로고
    • The mechanism of Bodian's silver staining: effect of copper ion on silver impregnation
    • Kondo H., Ikeda K., and Miyazaki N. The mechanism of Bodian's silver staining: effect of copper ion on silver impregnation. J. Neurosci. Methods 68 (1996) 275-280
    • (1996) J. Neurosci. Methods , vol.68 , pp. 275-280
    • Kondo, H.1    Ikeda, K.2    Miyazaki, N.3
  • 6
    • 0028219162 scopus 로고
    • A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels
    • Nesterenko M.V., Tilley M., and Upton S.J. A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels. J. Biochem. Biophys. Methods 28 (1994) 239-242
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 239-242
    • Nesterenko, M.V.1    Tilley, M.2    Upton, S.J.3
  • 7
    • 0025823838 scopus 로고
    • Staining and quantification of proteins separated by polyacrylamide gel electrophoresis
    • Syrovy I., and Hodny Z. Staining and quantification of proteins separated by polyacrylamide gel electrophoresis. J. Chromatogr. 569 (1991) 175-196
    • (1991) J. Chromatogr. , vol.569 , pp. 175-196
    • Syrovy, I.1    Hodny, Z.2
  • 8
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
    • Heukeshoven J., and Dernick R. Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 6 (1985) 103-112
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 9
    • 84988052094 scopus 로고
    • Simplified silver protein detection and image enhancement methods in polyacrylamide gels
    • Merril C.R., Goldman D., and Van Keuren M.L. Simplified silver protein detection and image enhancement methods in polyacrylamide gels. Electrophoresis 3 (1982) 17-23
    • (1982) Electrophoresis , vol.3 , pp. 17-23
    • Merril, C.R.1    Goldman, D.2    Van Keuren, M.L.3
  • 10
    • 0033662168 scopus 로고    scopus 로고
    • A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry
    • Yan J.X., Wait R., Berkelman T., Harry R.A., Westbrook J.A., Wheeler C.H., and Dunn M.J. A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry. Electrophoresis 21 (2000) 3666-3672
    • (2000) Electrophoresis , vol.21 , pp. 3666-3672
    • Yan, J.X.1    Wait, R.2    Berkelman, T.3    Harry, R.A.4    Westbrook, J.A.5    Wheeler, C.H.6    Dunn, M.J.7
  • 11
    • 33847648535 scopus 로고    scopus 로고
    • Formation of ε-formyllysine on silver-stained proteins: implications for assignment of isobaric dimethylation sites by tandem mass spectrometry
    • Oses-Prieto J.A., Zhang X., and Burlingame A.L. Formation of ε-formyllysine on silver-stained proteins: implications for assignment of isobaric dimethylation sites by tandem mass spectrometry. Mol. Cell Proteomics 6 (2007) 181-192
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 181-192
    • Oses-Prieto, J.A.1    Zhang, X.2    Burlingame, A.L.3
  • 12
    • 15944413138 scopus 로고    scopus 로고
    • Identification of dynamic proteome changes upon ligand activation of Trk-receptors using two-dimensional fluorescence difference gel electrophoresis and mass spectrometry
    • Sitek B., Apostolov O., Stuhler K., Pfeiffer K., Meyer H.E., Eggert A., and Schramm A. Identification of dynamic proteome changes upon ligand activation of Trk-receptors using two-dimensional fluorescence difference gel electrophoresis and mass spectrometry. Mol. Cell Proteomics 4 (2005) 291-299
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 291-299
    • Sitek, B.1    Apostolov, O.2    Stuhler, K.3    Pfeiffer, K.4    Meyer, H.E.5    Eggert, A.6    Schramm, A.7
  • 13
    • 0036243582 scopus 로고    scopus 로고
    • An improved formulation of SYPRO Ruby protein gel stain: comparison with the original formulation and with a ruthenium II tris(bathophenanthroline disulfonate) formulation
    • Berggren K.N., Schulenberg B., Lopez M.F., Steinberg T.H., Bogdanova A., Smejkal G., Wang A., and Patton W.F. An improved formulation of SYPRO Ruby protein gel stain: comparison with the original formulation and with a ruthenium II tris(bathophenanthroline disulfonate) formulation. Proteomics 2 (2000) 486-498
    • (2000) Proteomics , vol.2 , pp. 486-498
    • Berggren, K.N.1    Schulenberg, B.2    Lopez, M.F.3    Steinberg, T.H.4    Bogdanova, A.5    Smejkal, G.6    Wang, A.7    Patton, W.F.8
  • 14
    • 0033915670 scopus 로고    scopus 로고
    • Background-free, high-sensitivity staining of proteins in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gels using a luminescent ruthenium complex
    • Berggren K., Chernokalskaya E., Steinberg T.H., Kemper C., Lopez M.F., Diwu Z., Haugland R.P., and Patton W.F. Background-free, high-sensitivity staining of proteins in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gels using a luminescent ruthenium complex. Electrophoresis 21 (2000) 2509-2521
    • (2000) Electrophoresis , vol.21 , pp. 2509-2521
    • Berggren, K.1    Chernokalskaya, E.2    Steinberg, T.H.3    Kemper, C.4    Lopez, M.F.5    Diwu, Z.6    Haugland, R.P.7    Patton, W.F.8
  • 15
    • 3242773844 scopus 로고    scopus 로고
    • Plant proteome analysis by mass spectrometry: principles, problems, pitfalls, and recent developments
    • Chevalier F., Rofidal V., Vanova P., Bergoin A., and Rossignol M. Plant proteome analysis by mass spectrometry: principles, problems, pitfalls, and recent developments. Phytochemistry 65 (2004) 1499-1506
    • (2004) Phytochemistry , vol.65 , pp. 1499-1506
    • Chevalier, F.1    Rofidal, V.2    Vanova, P.3    Bergoin, A.4    Rossignol, M.5
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 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
  • 18
    • 0020215956 scopus 로고
    • A faithful double stain of proteins in the polyacrylamide gels with Coomassie blue and silver
    • Irie S., Sezaki M., and Kato Y. A faithful double stain of proteins in the polyacrylamide gels with Coomassie blue and silver. Anal. Biochem. 126 (1982) 350-354
    • (1982) Anal. Biochem. , vol.126 , pp. 350-354
    • Irie, S.1    Sezaki, M.2    Kato, Y.3
  • 19
    • 0022313128 scopus 로고
    • Silver staining of proteins in polyacrylamide gels: increased sensitivity through a combined Coomassie blue-silver stain procedure
    • De Moreno M.R., Smith J.F., and Smith R.V. Silver staining of proteins in polyacrylamide gels: increased sensitivity through a combined Coomassie blue-silver stain procedure. Anal. Biochem. 151 (1985) 466-470
    • (1985) Anal. Biochem. , vol.151 , pp. 466-470
    • De Moreno, M.R.1    Smith, J.F.2    Smith, R.V.3
  • 20
    • 0036961310 scopus 로고    scopus 로고
    • Background-free, fast protein staining in sodium dodecyl sulfate polyacrylamide gel using counterion dyes, zincon, and ethyl violet
    • Choi J.K., Tak K.H., Jin L.T., Hwang S.Y., Kwon T.I., and Yoo G.S. Background-free, fast protein staining in sodium dodecyl sulfate polyacrylamide gel using counterion dyes, zincon, and ethyl violet. Electrophoresis 23 (2002) 4053-4059
    • (2002) Electrophoresis , vol.23 , pp. 4053-4059
    • Choi, J.K.1    Tak, K.H.2    Jin, L.T.3    Hwang, S.Y.4    Kwon, T.I.5    Yoo, G.S.6
  • 21
    • 2342593283 scopus 로고    scopus 로고
    • Fast visible dye staining of proteins in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gels compatible with matrix assisted laser desorption/ionization-mass spectrometry
    • Choi J.K., Chae H.Z., Hwang S.Y., Choi H.I., Jin L.T., and Yoo G.S. Fast visible dye staining of proteins in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gels compatible with matrix assisted laser desorption/ionization-mass spectrometry. Electrophoresis 25 (2004) 1136-1141
    • (2004) Electrophoresis , vol.25 , pp. 1136-1141
    • Choi, J.K.1    Chae, H.Z.2    Hwang, S.Y.3    Choi, H.I.4    Jin, L.T.5    Yoo, G.S.6
  • 22
    • 0035356739 scopus 로고    scopus 로고
    • Proteolysis in mixed organic-aqueous solvent systems: applications for peptide mass mapping using mass spectrometry
    • Russell W.K., Park Z.Y., and Russell D.H. 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
  • 23
    • 0025053763 scopus 로고
    • Mechanisms of protein silver staining in polyacrylamide gels: a 10-year synthesis
    • Rabillound T. Mechanisms of protein silver staining in polyacrylamide gels: a 10-year synthesis. Electrophoresis 11 (1990) 785-794
    • (1990) Electrophoresis , vol.11 , pp. 785-794
    • Rabillound, T.1
  • 24
    • 0023825124 scopus 로고
    • Improved silver staining procedure for fast staining in PhastSystem Development Unit: I. Staining of sodium dodecyl sulfate gels
    • Heukeshoven J., and Dernick R. Improved silver staining procedure for fast staining in PhastSystem Development Unit: I. Staining of sodium dodecyl sulfate gels. Electrophoresis 9 (1988) 28-32
    • (1988) Electrophoresis , vol.9 , pp. 28-32
    • Heukeshoven, J.1    Dernick, R.2
  • 25
    • 0031729036 scopus 로고    scopus 로고
    • Mixed-dye staining method for protein detection in polyacrylamide gel electrophoresis using calconcarboxylic acid and rhodamine B
    • Jung D.W., Yoo G.S., and Choi J.K. Mixed-dye staining method for protein detection in polyacrylamide gel electrophoresis using calconcarboxylic acid and rhodamine B. Electrophoresis 19 (1998) 2412-2415
    • (1998) Electrophoresis , vol.19 , pp. 2412-2415
    • Jung, D.W.1    Yoo, G.S.2    Choi, J.K.3
  • 26
    • 0027451975 scopus 로고
    • Detection of proteins on polyacrylamide gels using calconcarboxylic acid
    • Hong H.Y., Choi J.K., and Yoo G.S. Detection of proteins on polyacrylamide gels using calconcarboxylic acid. Anal. Biochem. 214 (1993) 96-99
    • (1993) Anal. Biochem. , vol.214 , pp. 96-99
    • Hong, H.Y.1    Choi, J.K.2    Yoo, G.S.3
  • 27
    • 4444358788 scopus 로고    scopus 로고
    • Sensitive silver staining of protein in sodium dodecyl sulfate-polyacrylamide gels using an azo dye, calconcarboxylic acid, as a silver-ion sensitizer
    • Jin L.T., Hwang S.Y., Yoo G.S., and Choi J.K. Sensitive silver staining of protein in sodium dodecyl sulfate-polyacrylamide gels using an azo dye, calconcarboxylic acid, as a silver-ion sensitizer. Electrophoresis 25 (2004) 2494-2500
    • (2004) Electrophoresis , vol.25 , pp. 2494-2500
    • Jin, L.T.1    Hwang, S.Y.2    Yoo, G.S.3    Choi, J.K.4
  • 28
    • 0000969148 scopus 로고    scopus 로고
    • Reduction of silver ions to a colloid by Eriochrome Black T
    • Zhai X., and Efrima S. Reduction of silver ions to a colloid by Eriochrome Black T. J. Phys. Chem. 100 (1996) 1779-1785
    • (1996) J. Phys. Chem. , vol.100 , pp. 1779-1785
    • Zhai, X.1    Efrima, S.2
  • 30
    • 0041358797 scopus 로고    scopus 로고
    • Sample preparation for two-dimensional gel electrophoresis
    • Shaw M.M., and Riederer B.M. Sample preparation for two-dimensional gel electrophoresis. Proteomics 3 (2003) 1408-1417
    • (2003) Proteomics , vol.3 , pp. 1408-1417
    • Shaw, M.M.1    Riederer, B.M.2
  • 31
    • 0031808347 scopus 로고    scopus 로고
    • Electrophoresis-related protein modification: alkylation of carboxy residues revealed by mass spectrometry
    • Haebel S., Albrecht T., Sparbier K., Walden P., Korner R., and Steup M. Electrophoresis-related protein modification: alkylation of carboxy residues revealed by mass spectrometry. Electrophoresis 19 (1998) 679-686
    • (1998) Electrophoresis , vol.19 , pp. 679-686
    • Haebel, S.1    Albrecht, T.2    Sparbier, K.3    Walden, P.4    Korner, R.5    Steup, M.6


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