메뉴 건너뛰기




Volumn 9, Issue 5, 2010, Pages 2619-2629

Peptide mass fingerprinting after less specific In-gel proteolysis using MALDI-LTQ-orbitrap and 4-chloro-α-cyanocinnamic acid

Author keywords

CHCA; Chymotrypsin; ClCCA; Crystallization; Digestion; Elastase; Exclusion list; HCCA; In gel; Morphology; PI; PMF; Protease; Proteinase K; Trypsin

Indexed keywords

4 CHLORO ALPHA CYANOCINNAMIC ACID; CHYMOTRYPSIN; CINNAMIC ACID DERIVATIVE; ELASTASE; PROTEINASE K; TRYPSIN; UNCLASSIFIED DRUG;

EID: 77952052893     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr100055z     Document Type: Article
Times cited : (10)

References (37)
  • 1
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel, W. J.; Billeci, T. M.; Stults, J. T.; Wong, S. C.; Grimley, C.; Watanabe, C. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 5011-5015
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wong, S.C.4    Grimley, C.5    Watanabe, C.6
  • 2
    • 0042386240 scopus 로고    scopus 로고
    • Protein identification: The origins of peptide mass fingerprinting
    • Henzel, W. J.; Watanabe, C.; Stults, J. T. Protein identification: The origins of peptide mass fingerprinting J. Am. Soc. Mass Spectrom. 2003, 14, 931-942
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 931-942
    • Henzel, W.J.1    Watanabe, C.2    Stults, J.T.3
  • 3
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis
    • Rosenfeld, J.; Capdevielle, J.; Guillemot, J. C.; Ferrara, P. In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis Anal. Biochem. 1992, 203, 173-179
    • (1992) Anal. Biochem. , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 4
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A.; Wilm, M.; Vorm, O.; Mann, M. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels Anal. Chem. 1996, 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 5
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A.; Tomas, H.; Havlis, J.; Olsen, J. V.; Mann, M. In-gel digestion for mass spectrometric characterization of proteins and proteomes Nat. Protoc. 2006, 1, 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 6
    • 33645466243 scopus 로고    scopus 로고
    • Toward the complete membrane proteome: High coverage of integral membrane proteins through transmembrane peptide detection
    • Fischer, F.; Wolters, D.; Rögner, M.; Poetsch, A. Toward the complete membrane proteome: high coverage of integral membrane proteins through transmembrane peptide detection Mol. Cell Proteomics 2006, 5, 444-453
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 444-453
    • Fischer, F.1    Wolters, D.2    Rögner, M.3    Poetsch, A.4
  • 9
    • 4444320836 scopus 로고    scopus 로고
    • Proteolysis and mass spectrometric analysis of an integral membrane protein: Aquaporin 0
    • Han, J.; Schey, K. L. Proteolysis and mass spectrometric analysis of an integral membrane protein: aquaporin 0 J. Proteome Res. 2004, 3, 807-812
    • (2004) J. Proteome Res. , vol.3 , pp. 807-812
    • Han, J.1    Schey, K.L.2
  • 10
    • 73149094295 scopus 로고    scopus 로고
    • Membrane protein analysis using an improved peptic in-solution digestion protocol
    • Rietschel, B.; Bornemann, S.; Arrey, T. N.; Baeumlisberger, D.; Karas, M.; Meyer, B. Membrane protein analysis using an improved peptic in-solution digestion protocol Proteomics 2009, 9 (24) 5553-5557
    • (2009) Proteomics , vol.9 , Issue.24 , pp. 5553-5557
    • Rietschel, B.1    Bornemann, S.2    Arrey, T.N.3    Baeumlisberger, D.4    Karas, M.5    Meyer, B.6
  • 11
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C.; MacCoss, M. J.; Howell, K. E.; Yates, J. R., III. A method for the comprehensive proteomic analysis of membrane proteins Nat. Biotechnol. 2003, 21, 508-510
    • (2003) Nat. Biotechnol. , vol.21 , pp. 508-510
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates Iii, J.R.4
  • 12
    • 0035863653 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation by a combination of elastase digestion and neutral loss tandem mass spectrometry
    • Schlosser, A.; Pipkorn, R.; Bossemeyer, D.; Lehmann, W. D. Analysis of protein phosphorylation by a combination of elastase digestion and neutral loss tandem mass spectrometry Anal. Chem. 2001, 73, 170-176
    • (2001) Anal. Chem. , vol.73 , pp. 170-176
    • Schlosser, A.1    Pipkorn, R.2    Bossemeyer, D.3    Lehmann, W.D.4
  • 13
    • 0035997277 scopus 로고    scopus 로고
    • Identification of protein phosphorylation sites by combination of elastase digestion, immobilized metal affinity chromatography, and quadrupole-time of flight tandem mass spectrometry
    • Schlosser, A.; Bodem, J.; Bossemeyer, D.; Grummt, I.; Lehmann, W. D. Identification of protein phosphorylation sites by combination of elastase digestion, immobilized metal affinity chromatography, and quadrupole-time of flight tandem mass spectrometry Proteomics 2002, 2, 911-918
    • (2002) Proteomics , vol.2 , pp. 911-918
    • Schlosser, A.1    Bodem, J.2    Bossemeyer, D.3    Grummt, I.4    Lehmann, W.D.5
  • 14
    • 0036243462 scopus 로고    scopus 로고
    • Patchwork peptide sequencing: Extraction of sequence information from accurate mass data of peptide tandem mass spectra recorded at high resolution
    • Schlosser, A.; Lehmann, W. D. Patchwork peptide sequencing: Extraction of sequence information from accurate mass data of peptide tandem mass spectra recorded at high resolution Proteomics 2002, 2, 524-533
    • (2002) Proteomics , vol.2 , pp. 524-533
    • Schlosser, A.1    Lehmann, W.D.2
  • 15
    • 23744504888 scopus 로고    scopus 로고
    • Mapping of phosphorylation sites by a multi-protease approach with specific phosphopeptide enrichment and NanoLC-MS/MS analysis
    • Schlosser, A.; Vanselow, J. T.; Kramer, A. Mapping of phosphorylation sites by a multi-protease approach with specific phosphopeptide enrichment and NanoLC-MS/MS analysis Anal. Chem. 2005, 77, 5243-5250
    • (2005) Anal. Chem. , vol.77 , pp. 5243-5250
    • Schlosser, A.1    Vanselow, J.T.2    Kramer, A.3
  • 16
    • 58149119846 scopus 로고    scopus 로고
    • Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis
    • Wang, B.; Malik, R.; Nigg, E. A.; Korner, R. Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis Anal. Chem. 2008, 80, 9526-9533
    • (2008) Anal. Chem. , vol.80 , pp. 9526-9533
    • Wang, B.1    Malik, R.2    Nigg, E.A.3    Korner, R.4
  • 17
    • 67651004664 scopus 로고    scopus 로고
    • Protein phosphorylation influences proteolytic cleavage and kinase substrate properties exemplified by analysis of in vitro phosphorylated plasmodium falciparum glideosome-associated protein 45 by nano-ultra performance liquid chromatography-tandem mass spectrometry
    • Winter, D.; Kugelstadt, D.; Seidler, J.; Kappes, B.; Lehmann, W. D. Protein phosphorylation influences proteolytic cleavage and kinase substrate properties exemplified by analysis of in vitro phosphorylated plasmodium falciparum glideosome-associated protein 45 by nano-ultra performance liquid chromatography-tandem mass spectrometry Anal. Biochem. 2009, 393, 41-47
    • (2009) Anal. Biochem. , vol.393 , pp. 41-47
    • Winter, D.1    Kugelstadt, D.2    Seidler, J.3    Kappes, B.4    Lehmann, W.D.5
  • 18
    • 51049093616 scopus 로고    scopus 로고
    • Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex i
    • Galkin, A.; Meyer, B.; Wittig, I.; Karas, M.; Schägger, H.; Vinogradov, A.; Brandt, U. Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I J. Biol. Chem. 2008, 283, 20907-20913
    • (2008) J. Biol. Chem. , vol.283 , pp. 20907-20913
    • Galkin, A.1    Meyer, B.2    Wittig, I.3    Karas, M.4    Schägger, H.5    Vinogradov, A.6    Brandt, U.7
  • 19
    • 25144508697 scopus 로고    scopus 로고
    • A new approach in proteomics of wheat gluten: Combining chymotrypsin cleavage and matrix-assisted laser desorption/ionization quadrupole ion trap reflectron tandem mass spectrometry
    • Salplachta, J.; Marchetti, M.; Chmelík, J.; Allmaier, G. A new approach in proteomics of wheat gluten: combining chymotrypsin cleavage and matrix-assisted laser desorption/ionization quadrupole ion trap reflectron tandem mass spectrometry Rapid Commun. Mass Spectrom. 2005, 19, 2725-2728
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 2725-2728
    • Salplachta, J.1    Marchetti, M.2    Chmelík, J.3    Allmaier, G.4
  • 20
    • 67049155252 scopus 로고    scopus 로고
    • Taking advantage of nonspecific trypsin cleavages for the identification of seed storage proteins in cereals
    • Sergeant, K.; Pinheiro, C.; Hausman, J. F.; Ricardo, C. P.; Renaut, J. Taking advantage of nonspecific trypsin cleavages for the identification of seed storage proteins in cereals J. Proteome Res. 2009, 8, 3182-3190
    • (2009) J. Proteome Res. , vol.8 , pp. 3182-3190
    • Sergeant, K.1    Pinheiro, C.2    Hausman, J.F.3    Ricardo, C.P.4    Renaut, J.5
  • 21
    • 0037398266 scopus 로고    scopus 로고
    • Interfacing the orbitrap mass analyzer to an electrospray ion source
    • Hardman, M.; Makarov, A. A. Interfacing the orbitrap mass analyzer to an electrospray ion source Anal. Chem. 2003, 75, 1699-1705
    • (2003) Anal. Chem. , vol.75 , pp. 1699-1705
    • Hardman, M.1    Makarov, A.A.2
  • 23
    • 65249098989 scopus 로고    scopus 로고
    • Sequencing of single and double stranded RNA oligonucleotides by acid hydrolysis and MALDI mass spectrometry
    • Bahr, U.; Aygün, H.; Karas, M. Sequencing of single and double stranded RNA oligonucleotides by acid hydrolysis and MALDI mass spectrometry Anal. Chem. 2009, 81, 3173-3179
    • (2009) Anal. Chem. , vol.81 , pp. 3173-3179
    • Bahr, U.1    Aygün, H.2    Karas, M.3
  • 24
    • 70449354921 scopus 로고    scopus 로고
    • The benefit of combining nLC-MALDI-Orbitrap MS data with nLC-MALDI-TOF/TOF data for proteomic analyses employing elastase
    • Rietschel, B.; Baeumlisberger, D.; Arrey, T. N.; Bornemann, S.; Rohmer, M.; Schuerken, M.; Karas, M.; Meyer, B. The benefit of combining nLC-MALDI-Orbitrap MS data with nLC-MALDI-TOF/TOF data for proteomic analyses employing elastase J. Proteome Res. 2009, 8 (11) 5317-5324
    • (2009) J. Proteome Res. , vol.8 , Issue.11 , pp. 5317-5324
    • Rietschel, B.1    Baeumlisberger, D.2    Arrey, T.N.3    Bornemann, S.4    Rohmer, M.5    Schuerken, M.6    Karas, M.7    Meyer, B.8
  • 25
    • 0033214277 scopus 로고    scopus 로고
    • The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins
    • Krause, E.; Wenschuh, H.; Jungblut, P. R. The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins Anal. Chem. 1999, 71, 4160-4165
    • (1999) Anal. Chem. , vol.71 , pp. 4160-4165
    • Krause, E.1    Wenschuh, H.2    Jungblut, P.R.3
  • 26
    • 50449099939 scopus 로고    scopus 로고
    • 4-Chloro-α-cyanocinnamic acid is an advanced, rationally designed MALDI matrix
    • Jaskolla, T. W.; Lehmann, W. D.; Karas, M. 4-Chloro-α-cyanocinnamic acid is an advanced, rationally designed MALDI matrix Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 12200-12205
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 12200-12205
    • Jaskolla, T.W.1    Lehmann, W.D.2    Karas, M.3
  • 27
    • 64049088118 scopus 로고    scopus 로고
    • The new matrix 4-chloro-α-cyanocinnamic acid allows the detection of phosphatidylethanolamine chloramines by MALDI-TOF mass spectrometry
    • Jaskolla, T. W.; Fuchs, B.; Karas, M.; Schiller, J. The new matrix 4-chloro-α-cyanocinnamic acid allows the detection of phosphatidylethanolamine chloramines by MALDI-TOF mass spectrometry J. Am. Soc. Mass Spectrom. 2009, 20, 867-874
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 867-874
    • Jaskolla, T.W.1    Fuchs, B.2    Karas, M.3    Schiller, J.4
  • 28
    • 67650394372 scopus 로고    scopus 로고
    • Comparison between the matrices α-cyano-4-hydroxycinnamic acid and 4-chloro-α-cyanocinnamic acid for trypsin, chymotrypsin, and pepsin digestions by MALDI-TOF mass spectrometry
    • Jaskolla, T. W.; Papasotiriou, D. G.; Karas, M. Comparison between the matrices α-cyano-4-hydroxycinnamic acid and 4-chloro-α-cyanocinnamic acid for trypsin, chymotrypsin, and pepsin digestions by MALDI-TOF mass spectrometry J. Proteome Res. 2009, 8, 3588-3597
    • (2009) J. Proteome Res. , vol.8 , pp. 3588-3597
    • Jaskolla, T.W.1    Papasotiriou, D.G.2    Karas, M.3
  • 29
    • 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 1970, 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V.; Arold, N.; Taube, D.; Ehrhardt, W. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250 Electrophoresis 1988, 9, 255-262
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 31
    • 0037444512 scopus 로고    scopus 로고
    • Fast-response proteomics by accelerated in-gel digestion of proteins
    • Havlis, J.; Thomas, H.; Sebela, M.; Shevchenko, A. Fast-response proteomics by accelerated in-gel digestion of proteins Anal. Chem. 2003, 75, 1300-1306
    • (2003) Anal. Chem. , vol.75 , pp. 1300-1306
    • Havlis, J.1    Thomas, H.2    Sebela, M.3    Shevchenko, A.4
  • 32
    • 77952057004 scopus 로고    scopus 로고
    • UniProt Home page
    • UniProt Home page. http://www.uniprot.org.
  • 33
    • 0017056107 scopus 로고
    • Specificity of trypsin and alpha-chymotrypsin towards neutral substrates
    • Vajda, T.; Szabó, T. Specificity of trypsin and alpha-chymotrypsin towards neutral substrates Acta. Biochim. Biophys. Acad. Sci. Hung. 1976, 11, 287-294
    • (1976) Acta. Biochim. Biophys. Acad. Sci. Hung. , vol.11 , pp. 287-294
    • Vajda, T.1    Szabó, T.2
  • 34
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 1999, 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 35
    • 2742576125 scopus 로고    scopus 로고
    • Accuracy requirements for peptide characterization by monoisotopic molecular mass measurements
    • Zubarev, R. A.; Hkansson, P.; Sundqvist, B. Accuracy requirements for peptide characterization by monoisotopic molecular mass measurements Anal. Chem. 1996, 68, 4060-4063
    • (1996) Anal. Chem. , vol.68 , pp. 4060-4063
    • Zubarev, R.A.1    Hkansson, P.2    Sundqvist, B.3
  • 36
    • 2342593352 scopus 로고    scopus 로고
    • De novo sequencing, peptide composition analysis, and composition-based sequencing: A new strategy employing accurate mass determination by fourier transform ion cyclotron resonance mass spectrometry
    • Spengler, B. De novo sequencing, peptide composition analysis, and composition-based sequencing: a new strategy employing accurate mass determination by fourier transform ion cyclotron resonance mass spectrometry J. Am. Soc. Mass Spectrom. 2004, 15, 703-14
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 703-714
    • Spengler, B.1
  • 37
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser, K. R.; Baker, P.; Burlingame, A. L. Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching Anal. Chem. 1999, 71, 2871-82
    • (1999) Anal. Chem. , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.