메뉴 건너뛰기




Volumn 951, Issue , 2013, Pages 103-111

In-solution digestion of glycoproteins for glycopeptide-based mass analysis

Author keywords

Glycopeptide; In solution digestion; Mass spectrometry; Protein glycosylation

Indexed keywords

GLYCOPEPTIDE; GLYCOPROTEIN; PEPTIDE HYDROLASE;

EID: 84878637764     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-146-2_8     Document Type: Article
Times cited : (3)

References (31)
  • 1
    • 5444254250 scopus 로고    scopus 로고
    • Lectin-based structural glycomics: Glycoproteomics and glycan profiling
    • Hirabayashi J (2004) Lectin-based structural glycomics: glycoproteomics and glycan profiling. Glycoconj J 21:35-40
    • (2004) Glycoconj J , vol.21 , pp. 35-40
    • Hirabayashi, J.1
  • 2
    • 33845449090 scopus 로고    scopus 로고
    • Global methods for protein glycosylation analysis by mass spectrometry
    • Budnik BA, Lee RS, Steen JAJ (2006) Global methods for protein glycosylation analysis by mass spectrometry. Biochim Biophys Acta 1764:1870-1880
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1870-1880
    • Budnik, B.A.1    Lee, R.S.2    Steen, J.A.J.3
  • 3
    • 33750097998 scopus 로고    scopus 로고
    • The use of mass spectrometry for the proteomic analysis of glycosylation
    • Morelle W, Canis K, Chirat F, Faid V, Michalski JC (2006) The use of mass spectrometry for the proteomic analysis of glycosylation. Proteomics 6:3993-4015
    • (2006) Proteomics , vol.6 , pp. 3993-4015
    • Morelle, W.1    Canis, K.2    Chirat, F.3    Faid, V.4    Michalski, J.C.5
  • 4
    • 34447097453 scopus 로고    scopus 로고
    • Analysis of protein glycosylation by mass spectrometry
    • Morelle W, Michalski JC (2007) Analysis of protein glycosylation by mass spectrometry. Nat Protoc 2:1585-1602
    • (2007) Nat Protoc , vol.2 , pp. 1585-1602
    • Morelle, W.1    Michalski, J.C.2
  • 5
    • 48849109894 scopus 로고    scopus 로고
    • Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry
    • Calvano CD, Zambonin CG, Jensen ON (2008) Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry. J Proteomics 71:304-317
    • (2008) J Proteomics , vol.71 , pp. 304-317
    • Calvano, C.D.1    Zambonin, C.G.2    Jensen, O.N.3
  • 6
    • 51649085326 scopus 로고    scopus 로고
    • Mass spectrometry and the emerging field of glycomics
    • Zaia J (2008) Mass spectrometry and the emerging field of glycomics. Chem Biol 15:881-892
    • (2008) Chem Biol , vol.15 , pp. 881-892
    • Zaia, J.1
  • 7
    • 66149083648 scopus 로고    scopus 로고
    • Enrichment strategies for glycopeptides
    • Packer NH, Karlsson NG (eds). Humana Press, New York, NY
    • Ito S, Hayama K, Hirabayashi J (2009) Enrichment strategies for glycopeptides. In: Packer NH, Karlsson NG (eds) Glycomics: methods and protocols. Humana Press, New York, NY
    • (2009) Glycomics: Methods and Protocols
    • Ito, S.1    Hayama, K.2    Hirabayashi, J.3
  • 8
  • 9
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates JR, Ruse CI, Nakorchevsky A (2009) Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng 11:49-79
    • (2009) Annu Rev Biomed Eng , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 12
    • 33845417633 scopus 로고    scopus 로고
    • Strategies for analysis of glycoprotein glycosylation
    • Geyer H, Geyer R (2006) Strategies for analysis of glycoprotein glycosylation. Biochim Biophys Acta 1764:1853-1869
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1853-1869
    • Geyer, H.1    Geyer, R.2
  • 13
    • 70349286075 scopus 로고    scopus 로고
    • Glycomic analysis: An array of technologies
    • Krishnamoorthy L, Mahal LK (2009) Glycomic analysis: an array of technologies. ACS Chem Biol 4:715-732
    • (2009) ACS Chem Biol , vol.4 , pp. 715-732
    • Krishnamoorthy, L.1    Mahal, L.K.2
  • 14
    • 45549101708 scopus 로고    scopus 로고
    • Glycosylation sitespecific analysis of HIV envelope proteins (JRFL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility
    • Go EP, Irungu J, Zhang Y, Dalpathado DS, Liao HX, Sutherland LL, Alam SM, Haynes BF, Desaire H (2008) Glycosylation sitespecific analysis of HIV envelope proteins (JRFL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility. J Proteome Res 7:1660-1674
    • (2008) J Proteome Res , vol.7 , pp. 1660-1674
    • Go, E.P.1    Irungu, J.2    Zhang, Y.3    Dalpathado, D.S.4    Liao, H.X.5    Sutherland, L.L.6    Alam, S.M.7    Haynes, B.F.8    Desaire, H.9
  • 15
    • 48349109797 scopus 로고    scopus 로고
    • Comparison of HPLC/ESI-FTICR MS versus MALDI-TOF/TOF MS for glycopeptide analysis of a highly glycosylated HIV envelope glycoprotein
    • Irungu J, Go EP, Zhang Y, Dalpathado DS, Liao HX, Haynes BF, Desaire H (2008) Comparison of HPLC/ESI-FTICR MS versus MALDI-TOF/TOF MS for glycopeptide analysis of a highly glycosylated HIV envelope glycoprotein. J Am Soc Mass Spectrom 19:1209-1220
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 1209-1220
    • Irungu, J.1    Go, E.P.2    Zhang, Y.3    Dalpathado, D.S.4    Liao, H.X.5    Haynes, B.F.6    Desaire, H.7
  • 16
    • 42949172966 scopus 로고    scopus 로고
    • Maximizing coverage of glycosylation heterogeneity in MALDI-MS analysis of glycoproteins with up to 27 glycosylation sites
    • Zhang Y, Go EP, Desaire H (2008) Maximizing coverage of glycosylation heterogeneity in MALDI-MS analysis of glycoproteins with up to 27 glycosylation sites. Anal Chem 80:3144-3158
    • (2008) Anal Chem , vol.80 , pp. 3144-3158
    • Zhang, Y.1    Go, E.P.2    Desaire, H.3
  • 19
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • Wada Y, Tajiri M, Yoshida S (2004) Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics. Anal Chem 76: 6560-6565
    • (2004) Anal Chem , vol.76 , pp. 6560-6565
    • Wada, Y.1    Tajiri, M.2    Yoshida, S.3
  • 20
    • 28444460388 scopus 로고    scopus 로고
    • Differential analysis of site-specific glycans on plasma and cellular fibronectins: Application of a hydrophilic affinity method for glycopeptide enrichment
    • Tajiri M, Yoshida S, Wada Y (2005) Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment. Glycobiology 15:1332-1340
    • (2005) Glycobiology , vol.15 , pp. 1332-1340
    • Tajiri, M.1    Yoshida, S.2    Wada, Y.3
  • 22
    • 0012382504 scopus 로고    scopus 로고
    • Protein determination by UV absorption
    • Walker JM (ed). Humana Press, Totowa, NJ
    • Aitken A, Learmonth M (1996) Protein determination by UV absorption. In: Walker JM (ed) The protein protocols handbook, 2nd edn. Humana Press, Totowa, NJ
    • (1996) The Protein Protocols Handbook, 2nd Edn
    • Aitken, A.1    Learmonth, M.2
  • 23
    • 71549152820 scopus 로고    scopus 로고
    • Quantitation of protein
    • Burgess RR, Deutscher MP (eds). Academic, London, UK
    • Noble JE, Bailey MJA (2009) Quantitation of protein. In: Burgess RR, Deutscher MP (eds) Methods in enzymology, 2nd edn. Academic, London, UK
    • (2009) Methods in Enzymology, 2nd Edn
    • Noble, J.E.1    Bailey, M.J.A.2
  • 24
    • 0028360823 scopus 로고
    • A procedure for quantitative determination of tris(2-carboxyethyl) phosphine, an odorless reducing agent more stable and effective than dithiothreitol
    • Han JC, Han GY (1994) A procedure for quantitative determination of tris(2-carboxyethyl) phosphine, an odorless reducing agent more stable and effective than dithiothreitol. Anal Biochem 220:5-10
    • (1994) Anal Biochem , vol.220 , pp. 5-10
    • Han, J.C.1    Han, G.Y.2
  • 26
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • Olsen JV, Ong SE, Mann M (2004) Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol Cell Proteomics 3:608-614
    • (2004) Mol Cell Proteomics , vol.3 , pp. 608-614
    • Olsen, J.V.1    Ong, S.E.2    Mann, M.3
  • 27
    • 0035356739 scopus 로고    scopus 로고
    • Proteolysis in mixed organic-aqueous solvent systems: Applications for peptide mass mapping using mass spectrometry
    • Russell WK, Park ZY, Russell DH (2001) Proteolysis in mixed organic-aqueous solvent systems: applications for peptide mass mapping using mass spectrometry. Anal Chem 73:2682-2685
    • (2001) Anal Chem , vol.73 , pp. 2682-2685
    • Russell, W.K.1    Park, Z.Y.2    Russell, D.H.3
  • 28
    • 30044447894 scopus 로고    scopus 로고
    • Efficient and specific trypsin digestion of microgram to nanogram quantities of proteins in organic-aqueous solvent systems
    • Strader MB, Tabb DL, Hervey WJ, Pan CL, Hurst GB (2006) Efficient and specific trypsin digestion of microgram to nanogram quantities of proteins in organic-aqueous solvent systems. Anal Chem 78:125-134
    • (2006) Anal Chem , vol.78 , pp. 125-134
    • Strader, M.B.1    Tabb, D.L.2    Hervey, W.J.3    Pan, C.L.4    Hurst, G.B.5
  • 31
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski JR, Zougman A, Nagaraj N, Mann M (2009) Universal sample preparation method for proteome analysis. Nat Methods 6:359-362
    • (2009) Nat Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.