메뉴 건너뛰기




Volumn 24, Issue 3, 2013, Pages 132-153

Optimization of the β-elimination/michael addition chemistry on reversed-phase supports for mass spectrometry analysis of O-linked protein modifications

Author keywords

Alkaline phosphatase; Chemical targeted proteolysis; O GlcNAcylation; Phosphoprotein characterization; Serial solid phase derivatization; ZiptipC18 pipette tips

Indexed keywords

BETA N ACETYLGLUCOSAMINE PEPTIDE; CALCITONIN; CHOLECYSTOKININ; PEPTIDE; PHOSPHOPEPTIDE; PHOSPHOSERYL PEPTIDE; PHOSPHOTHREONYL PEPTIDE; UNCLASSIFIED DRUG; N ACETYLGLUCOSAMINE;

EID: 84883614316     PISSN: 15240215     EISSN: 19434731     Source Type: Journal    
DOI: 10.7171/jbt.13-2403-005     Document Type: Article
Times cited : (11)

References (51)
  • 1
    • 0033724701 scopus 로고    scopus 로고
    • Chaperones in cell cycle regulation and mitotic signal transduction: A review
    • Helmbrecht K, Zeise F, Rensing L. Chaperones in cell cycle regulation and mitotic signal transduction: a review. Cell Proliferation 2000;33:341-356.
    • (2000) Cell Proliferation , vol.33 , pp. 341-356
    • Helmbrecht, K.1    Zeise, F.2    Rensing, L.3
  • 2
    • 0029822412 scopus 로고    scopus 로고
    • Phosphopeptide analysis by matrix-assisted laser desorption time-of-flight mass spectrometry
    • Annan RS, Carr SA. Phosphopeptide analysis by matrix-assisted laser desorption time-of-flight mass spectrometry. Anal Chem 1996;68:3413-3421.
    • (1996) Anal Chem , vol.68 , pp. 3413-3421
    • Annan, R.S.1    Carr, S.A.2
  • 3
    • 0035253691 scopus 로고    scopus 로고
    • A multidimensional electrospray MS-based approach to phosphopeptide mapping
    • Annan RS, Huddleston MJ, Verma R, Deshaies RJ, Carr SA. A multidimensional electrospray MS-based approach to phosphopeptide mapping. Anal Chem 2001;73:393-404.
    • (2001) Anal Chem , vol.73 , pp. 393-404
    • Annan, R.S.1    Huddleston, M.J.2    Verma, R.3    Deshaies, R.J.4    Carr, S.A.5
  • 4
    • 0032995789 scopus 로고    scopus 로고
    • Electrospray tandem mass spectrometric studies of phosphopeptides and phosphopeptide analogues
    • Tholey A, Reed J, Lehmann W. Electrospray tandem mass spectrometric studies of phosphopeptides and phosphopeptide analogues. J Mass Spectrom 1999;34:117-123.
    • (1999) J Mass Spectrom , vol.34 , pp. 117-123
    • Tholey, A.1    Reed, J.2    Lehmann, W.3
  • 5
    • 0028362020 scopus 로고
    • An approach to locate phosphorylation sites in a phosphoprotein: Mass mapping by combining specific enzymatic degradation with matrix-assisted laser desorption/ionization mass spectrometry
    • Liao PC, Leykam J, Andrews PC, Gage DA, Allison J. An approach to locate phosphorylation sites in a phosphoprotein: mass mapping by combining specific enzymatic degradation with matrix-assisted laser desorption/ionization mass spectrometry. Anal Biochem 1994;219:9-20.
    • (1994) Anal Biochem , vol.219 , pp. 9-20
    • Liao, P.C.1    Leykam, J.2    Andrews, P.C.3    Gage, D.A.4    Allison, J.5
  • 6
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide micro columns
    • Larsen MR, Thingholm TE, Jense ON, Roepstorff P, Jorgensen JD. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide micro columns. Mol Cell Proteomics 2005;4:873-886.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jense, O.N.3    Roepstorff, P.4    Jorgensen, J.D.5
  • 7
    • 4344574540 scopus 로고    scopus 로고
    • Large-scale characterization of HeLa cell nuclear phosphoproteins
    • Beausoleil SA, Jedrychowki M., Schwartz D, et al. Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci USA 2004;101:12130-12135.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12130-12135
    • Beausoleil, S.A.1    Jedrychowki, M.2    Schwartz, D.3
  • 8
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina H, Horn DM, Tang N, Mathivanan S, Pandey A. Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci USA 2007;104:2199-2204.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 9
    • 83055182135 scopus 로고    scopus 로고
    • Evaluation of HCD- and CID-type fragmentation within their respective detection platforms for murine phosphoproteomics
    • 10:M111.009910
    • Jedrychowski MP, Huttlin EL, Haas W, Sowa ME, Rad R, Gygi SP. Evaluation of HCD- and CID-type fragmentation within their respective detection platforms for murine phosphoproteomics. Mol Cell Proteomics 2011;10:M111.009910.
    • (2011) Mol Cell Proteomics
    • Jedrychowski, M.P.1    Huttlin, E.L.2    Haas, W.3    Sowa, M.E.4    Rad, R.5    Gygi, S.P.6
  • 10
    • 0032542058 scopus 로고    scopus 로고
    • Characterization of serine and threonine phosphorylation in &β-elimination/ethanethiol addition-modified proteins by electrospray tandem mass spectrometry and database searching
    • Jaffe H, Veeranna, Harish CP. Characterization of serine and threonine phosphorylation in &β-elimination/ethanethiol addition-modified proteins by electrospray tandem mass spectrometry and database searching. Biochemistry 1998;37: 16211-16224.
    • (1998) Biochemistry , vol.37 , pp. 16211-16224
    • Jaffe, H.1    Veeranna2    Harish, C.P.3
  • 11
    • 0345731218 scopus 로고    scopus 로고
    • Characterization of protein kinase A phosphorylation: Multi-technique approach to phosphate mapping
    • Shen J, Smith RA, Stoll VS, et al. Characterization of protein kinase A phosphorylation: multi-technique approach to phosphate mapping. Anal Biochem 2004;324:204-218.
    • (2004) Anal Biochem , vol.324 , pp. 204-218
    • Shen, J.1    Smith, R.A.2    Stoll, V.S.3
  • 12
    • 0038337889 scopus 로고    scopus 로고
    • Characterization of protein phosphorylation by mass spectrometry using immobilized metal ion affinity chromatography with on-resin-elimination and Michael addition
    • Thompson AJ, Hart SR, Franz C, Barnouin K, Ridley A, Cramer R. Characterization of protein phosphorylation by mass spectrometry using immobilized metal ion affinity chromatography with on-resin-elimination and Michael addition. Anal Chem 2003;75:3232-3243.
    • (2003) Anal Chem , vol.75 , pp. 3232-3243
    • Thompson, A.J.1    Hart, S.R.2    Franz, C.3    Barnouin, K.4    Ridley, A.5    Cramer, R.6
  • 13
    • 33646716257 scopus 로고    scopus 로고
    • Applications of highly sensitive phosphopeptide derivatization methods without the need of organic solvents
    • Reinders J, Meyer HE, Sickman A. Applications of highly sensitive phosphopeptide derivatization methods without the need of organic solvents. Proteomics 2006;6:2647-2649.
    • (2006) Proteomics , vol.6 , pp. 2647-2649
    • Reinders, J.1    Meyer, H.E.2    Sickman, A.3
  • 15
    • 0346656828 scopus 로고    scopus 로고
    • Identification of phosphorylated and glycosylated sites in peptides by chemically targeted proteolysis
    • Rusnak F, Zhou J, Hathaway GM. Identification of phosphorylated and glycosylated sites in peptides by chemically targeted proteolysis. J Biomol Tech 2002;13:228-237.
    • (2002) J Biomol Tech , vol.13 , pp. 228-237
    • Rusnak, F.1    Zhou, J.2    Hathaway, G.M.3
  • 17
    • 84865773882 scopus 로고    scopus 로고
    • Phosphopeptide characterization by mass spectrometry using reversed-phase supports for solid-phase- βelimination/Michael addition
    • Nika H, Lee JH, Willis IM, Angeletti RH, Hawke DH. Phosphopeptide characterization by mass spectrometry using reversed-phase supports for solid-phase- βelimination/Michael addition. J Biomol Tech 2012;23:2012-2302.
    • (2012) J Biomol Tech , vol.23 , pp. 2012-2302
    • Nika, H.1    Lee, J.H.2    Willis, I.M.3    Angeletti, R.H.4    Hawke, D.H.5
  • 18
    • 0033989522 scopus 로고    scopus 로고
    • Microscale sample preparation
    • Pluskal MG. Microscale sample preparation. Nat Biotech 2000; 18:104-105.
    • (2000) Nat Biotech , vol.18 , pp. 104-105
    • Pluskal, M.G.1
  • 19
    • 84869489173 scopus 로고    scopus 로고
    • Sample cleanup by solid phase extraction/pipet-tip chromatography
    • 1st ed. Totowa, NJ, USA: Humana
    • Aitken A. Sample cleanup by solid phase extraction/pipet-tip chromatography. In Walker J (ed): The Proteomics Protocols Handbook, 1st ed. Totowa, NJ, USA: Humana, 2005;307-309.
    • (2005) The Proteomics Protocols Handbook , pp. 307-309
    • Aitken, A.1
  • 20
    • 33645734804 scopus 로고    scopus 로고
    • Sulfonation chemistry as a powerful tool for MALDI TOF/TOF de novo sequencing and posttranslational modification analysis
    • Conrotto P, Hellman U. Sulfonation chemistry as a powerful tool for MALDI TOF/TOF de novo sequencing and posttranslational modification analysis. J Biomol Tech 2005;16:441-452.
    • (2005) J Biomol Tech , vol.16 , pp. 441-452
    • Conrotto, P.1    Hellman, U.2
  • 21
    • 32544447058 scopus 로고    scopus 로고
    • Accelerated on-column lysine derivatization and cysteine methylation by imidazole reaction in a deuterated environment for enhanced product ion analysis
    • Cindric M, Cepo T, Skrlin A, Vuletic M, Bindila L. Accelerated on-column lysine derivatization and cysteine methylation by imidazole reaction in a deuterated environment for enhanced product ion analysis. Rapid Commun Mass Spectrom 2006;20:694-702.
    • (2006) Rapid Commun Mass Spectrom , vol.20 , pp. 694-702
    • Cindric, M.1    Cepo, T.2    Skrlin, A.3    Vuletic, M.4    Bindila, L.5
  • 22
    • 77953665453 scopus 로고    scopus 로고
    • IVICAT for masses: An improved technique for permethylation of peptides
    • Farmar JG, Nika H, Che F-Y, Weiss L, Hogue Angeletti R. IVICAT for masses: an improved technique for permethylation of peptides. J Biomol Tech 2009;20:285-292.
    • (2009) J Biomol Tech , vol.20 , pp. 285-292
    • Farmar, J.G.1    Nika, H.2    Che, F.-Y.3    Weiss, L.4    Angeletti, R.H.5
  • 23
    • 27444439372 scopus 로고    scopus 로고
    • The use of solid-phase supports for derivatization in chromatography and spectroscopy
    • Johnson ME, Carpenter TS. The use of solid-phase supports for derivatization in chromatography and spectroscopy. Appl Spectrosc Rev 2005;40:391-412.
    • (2005) Appl Spectrosc Rev , vol.40 , pp. 391-412
    • Johnson, M.E.1    Carpenter, T.S.2
  • 25
    • 34250878954 scopus 로고    scopus 로고
    • Mechanism of specificity in protein phosphorylation
    • Ubersax JA, Ferrrell JE. Mechanism of specificity in protein phosphorylation. Nat Rev Mol Cell Biol 2007;8:530-541.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 530-541
    • Ubersax, J.A.1    Ferrrell, J.E.2
  • 26
    • 0037351048 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1: A catalyst for oncogenesis and a potential therapeutic target in cancer
    • Ryo A, Liou Y-C, Lu KP, Wulf, G. Prolyl isomerase Pin1: a catalyst for oncogenesis and a potential therapeutic target in cancer. J Cell Sci 203;116:773-783.
    • J Cell Sci 203 , vol.116 , pp. 773-783
    • Ryo, A.1    Liou, Y.-C.2    Lu, K.P.3    Wulf, G.4
  • 27
    • 0037446738 scopus 로고    scopus 로고
    • Threonine phosphorylation sites in the β2 and β7 leucocyte integrin polypeptide
    • Hilden TJ, Valmu L, Karkainen S, Gahmberg CG. Threonine phosphorylation sites in the β2 and β7 leucocyte integrin polypeptide. J Immunol 2003;170:4170-4177.
    • (2003) J Immunol , vol.170 , pp. 4170-4177
    • Hilden, T.J.1    Valmu, L.2    Karkainen, S.3    Gahmberg, C.G.4
  • 28
    • 0035891038 scopus 로고    scopus 로고
    • Phosphopeptide derivatization signatures to identify serine and threonine phosphorylated peptides by mass spectrometry
    • Molloy MP, Andrews PC. Phosphopeptide derivatization signatures to identify serine and threonine phosphorylated peptides by mass spectrometry. Anal Chem 2001;73:5387-5394.
    • (2001) Anal Chem , vol.73 , pp. 5387-5394
    • Molloy, M.P.1    Andrews, P.C.2
  • 29
    • 0041920930 scopus 로고    scopus 로고
    • A new approach to phosphoserine and phosphothreonine analysis in peptides and proteins: Chemical modification, enrichment via solid-phase reversible binding, and analysis by mass spectrometry
    • Thaler F, Valsasina B, Baldi R, et al. A new approach to phosphoserine and phosphothreonine analysis in peptides and proteins: chemical modification, enrichment via solid-phase reversible binding, and analysis by mass spectrometry. Anal Bioanal Chem 2003;376:366-373.
    • (2003) Anal Bioanal Chem , vol.376 , pp. 366-373
    • Thaler, F.1    Valsasina, B.2    Baldi, R.3
  • 30
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • Wells L, Vosseller K, Cole RN, Cronshaw JM, Matunis MJ, Hart GW. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol Cell Proteomics 2002;1:791-804.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 31
    • 0002844767 scopus 로고    scopus 로고
    • Systematic analysis of peptide recoveries from in-gel digestions for protein identifications in proteome studies
    • Speicher DT, Kolbas O, Harper D, Speicher DW. Systematic analysis of peptide recoveries from in-gel digestions for protein identifications in proteome studies. J Biomol Tech 2000;11:74-86.
    • (2000) J Biomol Tech , vol.11 , pp. 74-86
    • Speicher, D.T.1    Kolbas, O.2    Harper, D.3    Speicher, D.W.4
  • 32
    • 0037090502 scopus 로고    scopus 로고
    • Optimization of guanidination procedures for MALDI mass mapping
    • Beardsley RL, Reilly JP. Optimization of guanidination procedures for MALDI mass mapping. Anal Chem 2002;74:1884-1890.
    • (2002) Anal Chem , vol.74 , pp. 1884-1890
    • Beardsley, R.L.1    Reilly, J.P.2
  • 33
    • 0035258294 scopus 로고    scopus 로고
    • Phospho-proteomics: Evaluation of the use of enzymatic dephosphorylation and differential mass spectrometric peptide mass mapping for site specific phosphorylation assignment in proteins separated by gel electrophoresis
    • Larsen MR, Sorensen GL, Fey SJ, Larsen PM, Roepstorff P. Phospho-proteomics: evaluation of the use of enzymatic dephosphorylation and differential mass spectrometric peptide mass mapping for site specific phosphorylation assignment in proteins separated by gel electrophoresis. Proteomics 2001;1: 223-238.
    • (2001) Proteomics , vol.1 , pp. 223-238
    • Larsen, M.R.1    Sorensen, G.L.2    Fey, S.J.3    Larsen, P.M.4    Roepstorff, P.5
  • 34
    • 1942470508 scopus 로고    scopus 로고
    • The contribution of specific amino acid side chains to signal intensities of peptides in matrix-assisted laser desorption/ ionization mass spectrometry
    • Baumgart S, Lindner Y, Kuhne R, Oberemm A, Wenschu H, Krause E. The contribution of specific amino acid side chains to signal intensities of peptides in matrix-assisted laser desorption/ ionization mass spectrometry. Rapid Commun Mass Spectrom 2004;18:863-868.
    • (2004) Rapid Commun Mass Spectrom , vol.18 , pp. 863-868
    • Baumgart, S.1    Lindner, Y.2    Kuhne, R.3    Oberemm, A.4    Wenschu, H.5    Krause, E.6
  • 36
    • 5444256180 scopus 로고    scopus 로고
    • Efficient in-gel digestion procedure using 5-cyclohexyl-1-pentyl-β-D-maltoside as an additive for gel-based membrane proteomics
    • Katayama H, Tabata T, Ishihama Y, Sato T, Oda Y, Nagasu T. Efficient in-gel digestion procedure using 5-cyclohexyl-1-pentyl-β-D-maltoside as an additive for gel-based membrane proteomics. Rapid Commun Mass Spectrom 2004;18:2388-2394.
    • (2004) Rapid Commun Mass Spectrom , vol.18 , pp. 2388-2394
    • Katayama, H.1    Tabata, T.2    Ishihama, Y.3    Sato, T.4    Oda, Y.5    Nagasu, T.6
  • 37
    • 33646900710 scopus 로고    scopus 로고
    • O-Linked N- acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry
    • Vosseller K., Trinidad JC, Chalkley RJ, et al. O-Linked N- acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry. Mol Cell Proteomics 2006;5:923-934.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 923-934
    • Vosseller, K.1    Trinidad, J.C.2    Chalkley, R.J.3
  • 38
    • 9144254626 scopus 로고    scopus 로고
    • Derivatization of phosphorylated peptides with S- and N-nucleophiles for enhanced ionization efficiency in matrix-assisted laser desorption/ionization mass spectrometry
    • Klemm C, Schroeder S, Gluckmann M, Beyermann M, Krause E. Derivatization of phosphorylated peptides with S- and N-nucleophiles for enhanced ionization efficiency in matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun Mass Spectrom 2004;18:2697-2705.
    • (2004) Rapid Commun Mass Spectrom , vol.18 , pp. 2697-2705
    • Klemm, C.1    Schroeder, S.2    Gluckmann, M.3    Beyermann, M.4    Krause, E.5
  • 39
    • 0016267353 scopus 로고
    • Kinetic studies on the alkali-catalyzed hydrolysis and epimerization of model alkyl and hydroxyalkyl di- and tripeptides
    • Noll BW, Jarboe CJ, Hass LF. Kinetic studies on the alkali-catalyzed hydrolysis and epimerization of model alkyl and hydroxyalkyl di- and tripeptides. Biochemistry 1974;13:5164-5169.
    • (1974) Biochemistry , vol.13 , pp. 5164-5169
    • Noll, B.W.1    Jarboe, C.J.2    Hass, L.F.3
  • 40
    • 2642545646 scopus 로고    scopus 로고
    • O-Sulfonation of serine and threonine: Mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes
    • Medzihradszky KF, Darula Z, Perlson E, et al. O-Sulfonation of serine and threonine: mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes. Mol Cell Proteomics 2004; 3:429-440.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 429-440
    • Medzihradszky, K.F.1    Darula, Z.2    Perlson, E.3
  • 41
    • 24144459552 scopus 로고    scopus 로고
    • Derivatization of phosphopeptides with mercapto- and aminofunctionalized conjugate groups by phosphate elimination and subsequent Michael addition
    • Mattila K, Siltainsuu J, Balaspiri L, Ora M, Lonnberg H. Derivatization of phosphopeptides with mercapto- and aminofunctionalized conjugate groups by phosphate elimination and subsequent Michael addition. Org Biomol Chem 2005;3:3039- 3044.
    • (2005) Org Biomol Chem , vol.3 , pp. 3039
    • Mattila, K.1    Siltainsuu, J.2    Balaspiri, L.3    Ora, M.4    Lonnberg, H.5
  • 43
    • 0242690399 scopus 로고    scopus 로고
    • Susceptibility of the hydroxyl groups in serine and threonine to β-elimination/Michael addition under commonly used moderately high-temperature conditions
    • Li W, Backlund PS, Boykins RA, Wang G, Chen K-C. Susceptibility of the hydroxyl groups in serine and threonine to β-elimination/Michael addition under commonly used moderately high-temperature conditions. Anal Biochem 2003;323:94-102.
    • (2003) Anal Biochem , vol.323 , pp. 94-102
    • Li, W.1    Backlund, P.S.2    Boykins, R.A.3    Wang, G.4    Chen, K.-C.5
  • 44
    • 0028816680 scopus 로고
    • High pH mobile phase effects on silica-based reversed-phase high-performance liquid chromatography
    • Kirkland JJ, van Straten MA, Claessens HA. High pH mobile phase effects on silica-based reversed-phase high-performance liquid chromatography. J Chromatogr A 1995;691:3-19.
    • (1995) J Chromatogr A , vol.691 , pp. 3-19
    • Kirkland, J.J.1    van Straten, M.A.2    Claessens, H.A.3
  • 45
    • 11844264844 scopus 로고    scopus 로고
    • Quantitation of binding, recovery and desalting efficiency of peptides and proteins in solid phase extraction micropipette tips
    • Palmblad M, Vogel JS. Quantitation of binding, recovery and desalting efficiency of peptides and proteins in solid phase extraction micropipette tips. J Chromatogr B 2005;814:309-313.
    • (2005) J Chromatogr B , vol.814 , pp. 309-313
    • Palmblad, M.1    Vogel, J.S.2
  • 46
    • 0036490141 scopus 로고    scopus 로고
    • Mass spectrometry-based methods for phosphorylation site mapping of hyperphosphorylated proteins applied to Net1, a regulator of exit from mitosis on yeast
    • Chen SL, Huddleston MJ, Shou W, Deshaies RJ, Annan RS, Carr SA. Mass spectrometry-based methods for phosphorylation site mapping of hyperphosphorylated proteins applied to Net1, a regulator of exit from mitosis on yeast. Mol Cell Proteomics 2002;1:186-196.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 186-196
    • Chen, S.L.1    Huddleston, M.J.2    Shou, W.3    Deshaies, R.J.4    Annan, R.S.5    Carr, S.A.6
  • 47
    • 0025893050 scopus 로고
    • The use of phosphopeptides to distinguish between protein phosphatase and acid/ alkaline phosphatase activities: Opposite effect specificity toward phosphoseryl/phosphothreonyl substrates
    • Donella-Deana A, Meyer HE, Pinna IA. The use of phosphopeptides to distinguish between protein phosphatase and acid/ alkaline phosphatase activities: opposite effect specificity toward phosphoseryl/phosphothreonyl substrates. Biochim Biophys Acta 1991;1094:130-133.
    • (1991) Biochim Biophys Acta , vol.1094 , pp. 130-133
    • Donella-Deana, A.1    Meyer, H.E.2    Pinna, I.A.3
  • 48
    • 0031408757 scopus 로고    scopus 로고
    • Peptide biotinylation with amine-reactive esters: Differential side chain reactivity
    • Miller BT, Collins TJ, Rogers ME, Kurosky A. Peptide biotinylation with amine-reactive esters: differential side chain reactivity. Peptides 1997;18:1585-1595.
    • (1997) Peptides , vol.18 , pp. 1585-1595
    • Miller, B.T.1    Collins, T.J.2    Rogers, M.E.3    Kurosky, A.4
  • 49
    • 0025670535 scopus 로고
    • Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation
    • Biemann K. Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation. Methods Enzymol 1990;193:455-479.
    • (1990) Methods Enzymol , vol.193 , pp. 455-479
    • Biemann, K.1
  • 50
    • 0033081238 scopus 로고    scopus 로고
    • Protein identification using 20-minute Edman cycles and sequence mixture analysis
    • Henzel W, Tropea J, Dupont D. Protein identification using 20-minute Edman cycles and sequence mixture analysis. Anal Biochem 1999;267:148-160.
    • (1999) Anal Biochem , vol.267 , pp. 148-160
    • Henzel, W.1    Tropea, J.2    Dupont, D.3
  • 51
    • 20644443909 scopus 로고    scopus 로고
    • Kinetic characterization of sequencing grade modified trypsin
    • Finehout EJ, Cantor JR, Lee KH. Kinetic characterization of sequencing grade modified trypsin. Proteomics 2005;5:2319-2321.
    • (2005) Proteomics , vol.5 , pp. 2319-2321
    • Finehout, E.J.1    Cantor, J.R.2    Lee, K.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.