메뉴 건너뛰기




Volumn 12, Issue 12, 2013, Pages 5666-5680

Comprehensive analysis of protein digestion using six trypsins reveals the origin of trypsin as a significant source of variability in proteomics

Author keywords

digestion; endoprotease specificity; label free quantification; mass spectrometry; missed cleavages; peptide abundance; proteomics; statistical analysis; trypsin; variability

Indexed keywords

HUMAN SERUM ALBUMIN; TRYPSIN; PEPTIDE FRAGMENT; SERUM ALBUMIN;

EID: 84890105210     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr400611h     Document Type: Article
Times cited : (66)

References (44)
  • 2
    • 79959424627 scopus 로고    scopus 로고
    • Quantitative, High-Resolution Proteomics for Data-Driven Systems Biology
    • Kornberg, R. D. Raetz, C. R. H. Rothman, J. E. Thorner, J. W. Annual Review: Palo Alto, CA
    • Cox, J.; Mann, M. Quantitative, High-Resolution Proteomics for Data-Driven Systems Biology. In Annual Review of Biochemistry; Kornberg, R. D.; Raetz, C. R. H.; Rothman, J. E.; Thorner, J. W., Eds.; Annual Review: Palo Alto, CA, 2011; Vol. 80, pp 273-299.
    • (2011) Annual Review of Biochemistry , vol.80 , pp. 273-299
    • Cox, J.1    Mann, M.2
  • 3
    • 79959485825 scopus 로고    scopus 로고
    • Bioanalytical approaches to analyzing peptides and proteins by LC-MS/MS
    • Ewles, M.; Goodwin, L. Bioanalytical approaches to analyzing peptides and proteins by LC-MS/MS Bioanalysis 2011, 3 (12) 1379-1397
    • (2011) Bioanalysis , vol.3 , Issue.12 , pp. 1379-1397
    • Ewles, M.1    Goodwin, L.2
  • 4
    • 79960108436 scopus 로고    scopus 로고
    • Comparability analysis of protein therapeutics by bottom-up LC-MS with stable isotope-tagged reference standards
    • Manuilov, A. V.; Radziejewski, C. H.; Lee, D. H. Comparability analysis of protein therapeutics by bottom-up LC-MS with stable isotope-tagged reference standards mAbs 2011, 3 (4) 387-395
    • (2011) MAbs , vol.3 , Issue.4 , pp. 387-395
    • Manuilov, A.V.1    Radziejewski, C.H.2    Lee, D.H.3
  • 5
    • 84555190746 scopus 로고    scopus 로고
    • Quantitation of therapeutic proteins following direct trypsin digestion of dried blood spot samples and detection by LC-MS-based bioanalytical methods in drug discovery
    • Olah, T. V.; Sleczka, B. G.; D'Arienzo, C.; Tymiak, A. A. Quantitation of therapeutic proteins following direct trypsin digestion of dried blood spot samples and detection by LC-MS-based bioanalytical methods in drug discovery Bioanalysis 2012, 4 (1) 29-40
    • (2012) Bioanalysis , vol.4 , Issue.1 , pp. 29-40
    • Olah, T.V.1    Sleczka, B.G.2    D'Arienzo, C.3    Tymiak, A.A.4
  • 6
    • 84865604070 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics
    • Bantscheff, M.; Kuster, B. Quantitative mass spectrometry in proteomics Anal. Bioanal. Chem. 2012, 404 (4) 937-8
    • (2012) Anal. Bioanal. Chem. , vol.404 , Issue.4 , pp. 937-938
    • Bantscheff, M.1    Kuster, B.2
  • 11
    • 79961202534 scopus 로고    scopus 로고
    • The importance of the digest: Proteolysis and absolute quantification in proteomics
    • Brownridge, P.; Beynon, R. J. The importance of the digest: Proteolysis and absolute quantification in proteomics Methods 2011, 54 (4) 351-360
    • (2011) Methods , vol.54 , Issue.4 , pp. 351-360
    • Brownridge, P.1    Beynon, R.J.2
  • 12
    • 84865576726 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: Critical review update from 2007 to the present
    • Bantscheff, M.; Lemeer, S.; Savitski, M. M.; Kuster, B. Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present Anal. Bioanal. Chem. 2012, 404 (4) 939-965
    • (2012) Anal. Bioanal. Chem. , vol.404 , Issue.4 , pp. 939-965
    • Bantscheff, M.1    Lemeer, S.2    Savitski, M.M.3    Kuster, B.4
  • 13
    • 84861990380 scopus 로고    scopus 로고
    • Selected reaction monitoring-based proteomics: Workflows, potential, pitfalls and future directions
    • Picotti, P.; Aebersold, R. Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions Nat. Methods 2012, 9 (6) 555-566
    • (2012) Nat. Methods , vol.9 , Issue.6 , pp. 555-566
    • Picotti, P.1    Aebersold, R.2
  • 14
    • 84861860481 scopus 로고    scopus 로고
    • Targeted Data Extraction of the MS/MS Spectra Generated by Data-independent Acquisition: A New Concept for Consistent and Accurate Proteome Analysis
    • Gillet, L. C.; Navarro, P.; Tate, S.; Rost, H.; Selevsek, N.; Reiter, L.; Bonner, R.; Aebersold, R. Targeted Data Extraction of the MS/MS Spectra Generated by Data-independent Acquisition: A New Concept for Consistent and Accurate Proteome Analysis Mol. Cell. Proteomics 2012, 11, (6)
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 6
    • Gillet, L.C.1    Navarro, P.2    Tate, S.3    Rost, H.4    Selevsek, N.5    Reiter, L.6    Bonner, R.7    Aebersold, R.8
  • 15
    • 84870389523 scopus 로고    scopus 로고
    • Pipeline to assess the greatest source of technical variance in quantitative proteomics using metabolic labelling
    • Russell, M. R.; Lilley, K. S. Pipeline to assess the greatest source of technical variance in quantitative proteomics using metabolic labelling J Proteomics 2012, 77, 441-54
    • (2012) J Proteomics , vol.77 , pp. 441-454
    • Russell, M.R.1    Lilley, K.S.2
  • 16
    • 79251520339 scopus 로고    scopus 로고
    • Variance component analysis of a multi-site study for the reproducibility of multiple reaction monitoring measurements of peptides in human plasma
    • Xia, J. Q.; Sedransk, N.; Feng, X. Variance component analysis of a multi-site study for the reproducibility of multiple reaction monitoring measurements of peptides in human plasma PLoS One 2011, 6 (1) e14590
    • (2011) PLoS One , vol.6 , Issue.1 , pp. 14590
    • Xia, J.Q.1    Sedransk, N.2    Feng, X.3
  • 18
    • 84855877960 scopus 로고    scopus 로고
    • Systematic and quantitative comparison of digest efficiency and specificity reveals the impact of trypsin quality on MS-based proteomics
    • Burkhart, J. M.; Schumbrutzki, C.; Wortelkamp, S.; Sickmann, A.; Zahedi, R. P. Systematic and quantitative comparison of digest efficiency and specificity reveals the impact of trypsin quality on MS-based proteomics J. Proteomics 2012, 75 (4) 1454-1462
    • (2012) J. Proteomics , vol.75 , Issue.4 , pp. 1454-1462
    • Burkhart, J.M.1    Schumbrutzki, C.2    Wortelkamp, S.3    Sickmann, A.4    Zahedi, R.P.5
  • 19
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • Olsen, J. V.; Ong, S. E.; Mann, M. Trypsin cleaves exclusively C-terminal to arginine and lysine residues Mol. Cell. Proteomics 2004, 3 (6) 608-14
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.6 , pp. 608-614
    • Olsen, J.V.1    Ong, S.E.2    Mann, M.3
  • 20
    • 0023474127 scopus 로고
    • Proteolysis Data Bank: Specificity of alpha-chymotrypsin from computation of protein cleavages
    • Keil, B. Proteolysis Data Bank: specificity of alpha-chymotrypsin from computation of protein cleavages Protein Sequences Data Anal. 1987, 1 (1) 13-20
    • (1987) Protein Sequences Data Anal. , vol.1 , Issue.1 , pp. 13-20
    • Keil, B.1
  • 23
    • 77949786295 scopus 로고    scopus 로고
    • Value of using multiple proteases for large-scale mass spectrometry-based proteomics
    • Swaney, D. L.; Wenger, C. D.; Coon, J. J. Value of using multiple proteases for large-scale mass spectrometry-based proteomics J. Proteome Res. 2010, 9 (3) 1323-9
    • (2010) J. Proteome Res. , vol.9 , Issue.3 , pp. 1323-1329
    • Swaney, D.L.1    Wenger, C.D.2    Coon, J.J.3
  • 24
    • 79955417151 scopus 로고    scopus 로고
    • Addressing trypsin bias in large scale (phospho)proteome analysis by size exclusion chromatography and secondary digestion of large post-trypsin peptides
    • Tran, B. Q.; Hernandez, C.; Waridel, P.; Potts, A.; Barblan, J.; Lisacek, F.; Quadroni, M. Addressing trypsin bias in large scale (phospho)proteome analysis by size exclusion chromatography and secondary digestion of large post-trypsin peptides J. Proteome Res. 2011, 10 (2) 800-11
    • (2011) J. Proteome Res. , vol.10 , Issue.2 , pp. 800-811
    • Tran, B.Q.1    Hernandez, C.2    Waridel, P.3    Potts, A.4    Barblan, J.5    Lisacek, F.6    Quadroni, M.7
  • 25
    • 80052973869 scopus 로고    scopus 로고
    • An assessment of the ultrasonic probe-based enhancement of protein cleavage with immobilized trypsin
    • Vale, G.; Santos, H. M.; Carreira, R. J.; Fonseca, L.; Miró, M.; Cerdà, V.; Reboiro-Jato, M.; Capelo, J. L. An assessment of the ultrasonic probe-based enhancement of protein cleavage with immobilized trypsin Proteomics 2011, 11 (19) 3866-3876
    • (2011) Proteomics , vol.11 , Issue.19 , pp. 3866-3876
    • Vale, G.1    Santos, H.M.2    Carreira, R.J.3    Fonseca, L.4    Miró, M.5    Cerdà, V.6    Reboiro-Jato, M.7    Capelo, J.L.8
  • 26
    • 77149121079 scopus 로고    scopus 로고
    • Nanobiocatalysis for protein digestion in proteomic analysis
    • Kim, J.; Kim, B. C.; Lopez-Ferrer, D.; Petritis, K.; Smith, R. D. Nanobiocatalysis for protein digestion in proteomic analysis Proteomics 2010, 10 (4) 687-699
    • (2010) Proteomics , vol.10 , Issue.4 , pp. 687-699
    • Kim, J.1    Kim, B.C.2    Lopez-Ferrer, D.3    Petritis, K.4    Smith, R.D.5
  • 27
    • 84862012968 scopus 로고    scopus 로고
    • The Effect of Pre-Analytical Variability on the Measurement of MRM-MS-Based Mid- to High-Abundance Plasma Protein Biomarkers and a Panel of Cytokines
    • Aguilar-Mahecha, A.; Kuzyk, M. A.; Domanski, D.; Borchers, C. H.; Basik, M. The Effect of Pre-Analytical Variability on the Measurement of MRM-MS-Based Mid- to High-Abundance Plasma Protein Biomarkers and a Panel of Cytokines PLoS One 2012, 7, (6)
    • (2012) PLoS One , vol.7 , pp. 6
    • Aguilar-Mahecha, A.1    Kuzyk, M.A.2    Domanski, D.3    Borchers, C.H.4    Basik, M.5
  • 28
    • 77957344363 scopus 로고    scopus 로고
    • A Quantitative Study of the Effects of Chaotropic Agents, Surfactants, and Solvents on the Digestion Efficiency of Human Plasma Proteins by Trypsin
    • Proc, J. L.; Kuzyk, M. A.; Hardie, D. B.; Yang, J.; Smith, D. S.; Jackson, A. M.; Parker, C. E.; Borchers, C. H. A Quantitative Study of the Effects of Chaotropic Agents, Surfactants, and Solvents on the Digestion Efficiency of Human Plasma Proteins by Trypsin J. Proteome Res. 2010, 9 (10) 5422-5437
    • (2010) J. Proteome Res. , vol.9 , Issue.10 , pp. 5422-5437
    • Proc, J.L.1    Kuzyk, M.A.2    Hardie, D.B.3    Yang, J.4    Smith, D.S.5    Jackson, A.M.6    Parker, C.E.7    Borchers, C.H.8
  • 29
    • 84859439966 scopus 로고    scopus 로고
    • Internal standards in the quantitative determination of protein biopharmaceuticals using liquid chromatography coupled to mass spectrometry
    • Bronsema, K. J.; Bischoff, R.; van de Merbel, N. C. Internal standards in the quantitative determination of protein biopharmaceuticals using liquid chromatography coupled to mass spectrometry J. Chromatogr., B 2012, 893, 1-14
    • (2012) J. Chromatogr., B , vol.893 , pp. 1-14
    • Bronsema, K.J.1    Bischoff, R.2    Van De Merbel, N.C.3
  • 30
    • 82755181913 scopus 로고    scopus 로고
    • Proteomics under Pressure: Development of Essential Sample Preparation Techniques in Proteomics Using Ultrahigh Hydrostatic Pressure
    • Freeman, E.; Ivanov, A. R. Proteomics under Pressure: Development of Essential Sample Preparation Techniques in Proteomics Using Ultrahigh Hydrostatic Pressure J. Proteome Res. 2011, 10 (12) 5536-5546
    • (2011) J. Proteome Res. , vol.10 , Issue.12 , pp. 5536-5546
    • Freeman, E.1    Ivanov, A.R.2
  • 31
    • 84868327851 scopus 로고    scopus 로고
    • Large-Scale Quantitative Assessment of Different In-Solution Protein Digestion Protocols Reveals Superior Cleavage Efficiency of Tandem Lys-C/Trypsin Proteolysis over Trypsin Digestion
    • Glatter, T.; Ludwig, C.; Ahrne, E.; Aebersold, R.; Heck, A. J. R.; Schmidt, A. Large-Scale Quantitative Assessment of Different In-Solution Protein Digestion Protocols Reveals Superior Cleavage Efficiency of Tandem Lys-C/Trypsin Proteolysis over Trypsin Digestion J. Proteome Res. 2012, 11 (11) 5145-5156
    • (2012) J. Proteome Res. , vol.11 , Issue.11 , pp. 5145-5156
    • Glatter, T.1    Ludwig, C.2    Ahrne, E.3    Aebersold, R.4    Heck, A.J.R.5    Schmidt, A.6
  • 32
    • 34548150256 scopus 로고    scopus 로고
    • Comparison of digestion protocols for microgram quantities of enriched protein samples
    • Hervey, W. J.; Strader, M. B.; Hurst, G. B. Comparison of digestion protocols for microgram quantities of enriched protein samples J. Proteome Res. 2007, 6 (8) 3054-3061
    • (2007) J. Proteome Res. , vol.6 , Issue.8 , pp. 3054-3061
    • Hervey, W.J.1    Strader, M.B.2    Hurst, G.B.3
  • 34
    • 33644856320 scopus 로고    scopus 로고
    • Effects of modified digestion schemes on the identification of proteins from complex mixtures
    • Klammer, A. A.; MacCoss, M. J. Effects of modified digestion schemes on the identification of proteins from complex mixtures J. Proteome Res. 2006, 5 (3) 695-700
    • (2006) J. Proteome Res. , vol.5 , Issue.3 , pp. 695-700
    • Klammer, A.A.1    MacCoss, M.J.2
  • 36
    • 84855353901 scopus 로고    scopus 로고
    • High efficiency and quantitatively reproducible protein digestion by trypsin-immobilized magnetic microspheres
    • Sun, L. L.; Li, Y. H.; Yang, P.; Zhu, G. J.; Dovichi, N. J. High efficiency and quantitatively reproducible protein digestion by trypsin-immobilized magnetic microspheres J. Chromatogr., A 2012, 1220, 68-74
    • (2012) J. Chromatogr., A , vol.1220 , pp. 68-74
    • Sun, L.L.1    Li, Y.H.2    Yang, P.3    Zhu, G.J.4    Dovichi, N.J.5
  • 37
    • 84858725817 scopus 로고    scopus 로고
    • Consecutive Proteolytic Digestion in an Enzyme Reactor Increases Depth of Proteomic and Phosphoproteomic Analysis
    • Wisniewski, J. R.; Mann, M. Consecutive Proteolytic Digestion in an Enzyme Reactor Increases Depth of Proteomic and Phosphoproteomic Analysis Anal. Chem. 2012, 84 (6) 2631-2637
    • (2012) Anal. Chem. , vol.84 , Issue.6 , pp. 2631-2637
    • Wisniewski, J.R.1    Mann, M.2
  • 38
    • 84855877960 scopus 로고    scopus 로고
    • Systematic and quantitative comparison of digest efficiency and specificity reveals the impact of trypsin quality on MS-based proteomics
    • Burkhart, J. M.; Schumbrutzki, C.; Wortelkamp, S.; Sickmann, A.; Zahedi, R. P. Systematic and quantitative comparison of digest efficiency and specificity reveals the impact of trypsin quality on MS-based proteomics J. Proteomics 2012, 75 (4) 1454-62
    • (2012) J. Proteomics , vol.75 , Issue.4 , pp. 1454-1462
    • Burkhart, J.M.1    Schumbrutzki, C.2    Wortelkamp, S.3    Sickmann, A.4    Zahedi, R.P.5
  • 39
    • 84881166708 scopus 로고    scopus 로고
    • Cutting Edge Proteomics: Benchmarking of Six Commercial Trypsins
    • Bunkenborg, J.; Espadas, G.; Molina, H. Cutting Edge Proteomics: Benchmarking of Six Commercial Trypsins J. Proteome Res. 2013, 12, 3631-41
    • (2013) J. Proteome Res. , vol.12 , pp. 3631-3641
    • Bunkenborg, J.1    Espadas, G.2    Molina, H.3
  • 41
    • 77449122863 scopus 로고    scopus 로고
    • Trans-proteomic pipeline: A pipeline for proteomic analysis
    • Pedrioli, P. G. Trans-proteomic pipeline: a pipeline for proteomic analysis Methods Mol. Biol. 2010, 604, 213-38
    • (2010) Methods Mol. Biol. , vol.604 , pp. 213-238
    • Pedrioli, P.G.1
  • 42
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom, L. Serine protease mechanism and specificity Chem. Rev. 2002, 102 (12) 4501-24
    • (2002) Chem. Rev. , vol.102 , Issue.12 , pp. 4501-4524
    • Hedstrom, L.1
  • 43
    • 84873363142 scopus 로고    scopus 로고
    • In-source fragmentation and the sources of partially tryptic peptides in shotgun proteomics
    • Kim, J. S.; Monroe, M. E.; Camp, D. G., 2nd; Smith, R. D.; Qian, W. J. In-source fragmentation and the sources of partially tryptic peptides in shotgun proteomics J. Proteome Res. 2013, 12 (2) 910-6
    • (2013) J. Proteome Res. , vol.12 , Issue.2 , pp. 910-916
    • Kim, J.S.1    Monroe, M.E.2    Camp II, D.G.3    Smith, R.D.4    Qian, W.J.5
  • 44
    • 84866294361 scopus 로고    scopus 로고
    • Prediction of missed proteolytic cleavages for the selection of surrogate peptides for quantitative proteomics
    • Lawless, C.; Hubbard, S. J. Prediction of missed proteolytic cleavages for the selection of surrogate peptides for quantitative proteomics OMICS 2012, 16 (9) 449-56
    • (2012) OMICS , vol.16 , Issue.9 , pp. 449-456
    • Lawless, C.1    Hubbard, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.