메뉴 건너뛰기




Volumn 446, Issue 1, 2014, Pages 28-36

Comparison of two approaches for quantitative O-linked glycan analysis used in characterization of recombinant proteins

Author keywords

HILIC; LTQ FT MS; O linked glycan analysis

Indexed keywords

AMMONIA; GLYCOPROTEINS; HYDROPHILICITY; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; REAGENTS; RECOMBINANT PROTEINS;

EID: 84888226286     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2013.10.019     Document Type: Article
Times cited : (16)

References (45)
  • 1
    • 77949266037 scopus 로고    scopus 로고
    • Carbohydrate analysis throughout the development of a protein therapeutic
    • E. Higgins Carbohydrate analysis throughout the development of a protein therapeutic Glycoconjugate J. 27 2010 211 225
    • (2010) Glycoconjugate J. , vol.27 , pp. 211-225
    • Higgins, E.1
  • 2
    • 0014408452 scopus 로고
    • Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins
    • D.M. Carlson Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins J. Biol. Chem. 243 1968 616 626
    • (1968) J. Biol. Chem. , vol.243 , pp. 616-626
    • Carlson, D.M.1
  • 3
    • 0016245734 scopus 로고
    • Structure of the O-glycosidically linked carbohydrate units of fetuin
    • R.G. Spiro, and V.D. Bhoyroo Structure of the O-glycosidically linked carbohydrate units of fetuin J. Biol. Chem. 249 1974 5704 5717
    • (1974) J. Biol. Chem. , vol.249 , pp. 5704-5717
    • Spiro, R.G.1    Bhoyroo, V.D.2
  • 4
    • 0028673927 scopus 로고
    • Neoglycolipids: Probes in structure/function assignments to oligosaccharides
    • T. Feizi, and R.A. Childs Neoglycolipids: probes in structure/function assignments to oligosaccharides Methods Enzymol. 242 1994 205 217
    • (1994) Methods Enzymol. , vol.242 , pp. 205-217
    • Feizi, T.1    Childs, R.A.2
  • 5
    • 33744467070 scopus 로고    scopus 로고
    • Mass spectrometric profiling of O-linked glycans released directly from glycoproteins in gels using in-gel reductive β-elimination
    • DOI 10.1002/pmic.200500331
    • A.M. Taylor, O. Holst, and J. Thomas-Oates Mass spectrometric profiling of O-linked glycans released directly from glycoproteins in gels using in-gel reductive β-elimination Proteomics 6 2006 2936 2946 (Pubitemid 43806392)
    • (2006) Proteomics , vol.6 , Issue.10 , pp. 2936-2946
    • Taylor, A.M.1    Holst, O.2    Thomas-Oates, J.3
  • 6
    • 0030025149 scopus 로고    scopus 로고
    • Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry
    • DOI 10.1006/abio.1996.0047
    • K.D. Greis, B.K. Hayes, F.I. Comer, M. Kirk, S. Barnes, T.L. Lowary, and G.W. Hart Selective detection and site analysis of O-GlcNAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry Anal. Biochem. 234 1996 38 49 (Pubitemid 26045751)
    • (1996) Analytical Biochemistry , vol.234 , Issue.1 , pp. 38-49
    • Greis, K.D.1    Hayes, B.K.2    Comer, F.I.3    Kirk, M.4    Barnes, S.5    Lowary, T.L.6    Hart, G.W.7
  • 7
    • 0018169814 scopus 로고
    • The sugar chain structures of ABO blood group active glycoproteins obtained from human erythrocyte membrane
    • S. Takasaki, K. Yamashita, and A. Kobata The sugar chain structures of ABO blood group active glycoproteins obtained from human erythrocyte membrane J. Biol. Chem. 253 1978 6086 6091 (Pubitemid 9014250)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.17 , pp. 6086-6091
    • Takasaki, S.1    Yamashita, K.2    Kobata, A.3
  • 8
    • 0037096068 scopus 로고    scopus 로고
    • Analysis of O-linked reducing oligosaccharides released by an in-line flow system
    • DOI 10.1006/abio.2002.5657
    • N.G. Karlsson, and N.H. Packer Analysis of O-linked reducing oligosaccharides released by an in-line flow system Anal. Biochem. 305 2002 173 185 (Pubitemid 34666790)
    • (2002) Analytical Biochemistry , vol.305 , Issue.2 , pp. 173-185
    • Karlsson, N.G.1    Packer, N.H.2
  • 9
    • 84989069128 scopus 로고
    • Determination of glycosylation sites in O-linked glycopeptides: A sensitive mass spectrometric protocol
    • G.J. Rademaker, J. Haverkamp, and J.E. Thomas-Oates Determination of glycosylation sites in O-linked glycopeptides: a sensitive mass spectrometric protocol Org. Mass Spectrom. 28 1993 1536 1541
    • (1993) Org. Mass Spectrom. , vol.28 , pp. 1536-1541
    • Rademaker, G.J.1    Haverkamp, J.2    Thomas-Oates, J.E.3
  • 10
    • 0025995521 scopus 로고
    • High-performance anion-exchange chromatography of neutral milk oligosaccharides and oligosaccharide alditols derived from mucin glycoproteins
    • G.P. Reddy, and C.A. Bush High-performance anion-exchange chromatography of neutral milk oligosaccharides and oligosaccharide alditols derived from mucin glycoproteins Anal. Biochem. 198 1991 278 284
    • (1991) Anal. Biochem. , vol.198 , pp. 278-284
    • Reddy, G.P.1    Bush, C.A.2
  • 11
    • 0031260488 scopus 로고    scopus 로고
    • Analysis of O-linked oligosaccharide alditols by high-pH anion-exchange chromatography with pulsed amperometric detection
    • DOI 10.1006/abio.1997.2300
    • N. Kotani, and S. Takasaki Analysis of O-linked oligosaccharide alditols by high-pH anion-exchange chromatography with pulsed amperometric detection Anal. Biochem. 252 1997 40 47 (Pubitemid 27408690)
    • (1997) Analytical Biochemistry , vol.252 , Issue.1 , pp. 40-47
    • Kotani, N.1    Takasaki, S.2
  • 12
    • 44949259176 scopus 로고    scopus 로고
    • Use of high-performance anion exchange chromatography with pulsed amperometric detection for O-glycan determination in yeast
    • DOI 10.1038/nprot.2008.76, PII NPROT.2008.76
    • T.A. Stadheim, H. Li, W. Kett, I.N. Burnina, and T.U. Gerngross Use of high-performance anion-exchange chromatography with pulsed amperometric detection for O-glycan determination in yeast Nat. Protoc. 3 2008 1026 1031 (Pubitemid 351818691)
    • (2008) Nature Protocols , vol.3 , Issue.6 , pp. 1026-1031
    • Stadheim, T.A.1    Li, H.2    Kett, W.3    Burnina, I.N.4    Gerngross, T.U.5
  • 13
    • 0026336894 scopus 로고
    • High performance anion-exchange chromatography of reduced oligosaccharides from sialomucins
    • K.O. Lloyd, and A. Savage High performance anion-exchange chromatography of reduced oligosaccharides from sialomucins Glycoconjugate J. 8 1991 493 498
    • (1991) Glycoconjugate J. , vol.8 , pp. 493-498
    • Lloyd, K.O.1    Savage, A.2
  • 14
    • 0027276403 scopus 로고
    • Separation and identification of O-linked oligosaccharides derived from glycoproteins by high-pH anion-exchange chromatography
    • DOI 10.1006/abio.1993.1235
    • T. Hayase, M. Sheykhanazari, V.P. Bhavanandan, A.V. Savage, and Y.C. Lee Separation and identification of O-linked oligosaccharides derived from glycoproteins by high-pH anion-exchange chromatography Anal. Biochem. 211 1993 72 80 (Pubitemid 23189332)
    • (1993) Analytical Biochemistry , vol.211 , Issue.1 , pp. 72-80
    • Hayase, T.1    Sheykhanazari, M.2    Bhavanandan, V.P.3    Savage, A.V.4    Lee, Y.C.5
  • 15
    • 0023788003 scopus 로고
    • New methods for rapid separation and detection of oligosaccharides from glycoproteins
    • L.M. Chen, M.G. Yet, and M.C. Shao New methods for rapid separation and detection of oligosaccharides from glycoproteins FASEB J. 2 1988 2819 2824
    • (1988) FASEB J. , vol.2 , pp. 2819-2824
    • Chen, L.M.1    Yet, M.G.2    Shao, M.C.3
  • 16
    • 0342976375 scopus 로고
    • Separation of positional isomers of oligosaccharides and glycopeptides by high-performance anion-exchange chromatography with pulsed amperometric detection
    • M.R. Hardy, and R.R. Townsend Separation of positional isomers of oligosaccharides and glycopeptides by high-performance anion-exchange chromatography with pulsed amperometric detection Proc. Natl. Acad. Sci. USA 85 1988 3289 3293
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3289-3293
    • Hardy, M.R.1    Townsend, R.R.2
  • 17
    • 0032524093 scopus 로고    scopus 로고
    • Structural analysis of O-linked oligosaccharide-alditols by electrospray-tandem mass spectrometry after mild periodate oxidation and derivatization with 2-aminopyridine
    • DOI 10.1006/abio.1998.2618
    • W. Morelle, J. Lemoine, and G. Strecker Structural analysis of O-linked oligosaccharide-alditols by electrospray tandem mass spectrometry after mild periodate oxidation and derivatization with 2-aminopyridine Anal. Biochem. 259 1998 16 27 (Pubitemid 28247045)
    • (1998) Analytical Biochemistry , vol.259 , Issue.1 , pp. 16-27
    • Morelle, W.1    Lemoine, J.2    Strecker, G.3
  • 20
    • 78449307982 scopus 로고    scopus 로고
    • Effect and limitation of excess ammonium on the release of O-glycans in reducing forms from glycoproteins under mild alkaline conditions for glycomic and functional analysis
    • G. Yu, Y. Zhang, Z. Zhang, L. Song, P. Wang, and W. Chai Effect and limitation of excess ammonium on the release of O-glycans in reducing forms from glycoproteins under mild alkaline conditions for glycomic and functional analysis Anal. Chem. 82 2010 9534 9542
    • (2010) Anal. Chem. , vol.82 , pp. 9534-9542
    • Yu, G.1    Zhang, Y.2    Zhang, Z.3    Song, L.4    Wang, P.5    Chai, W.6
  • 21
    • 0035894307 scopus 로고    scopus 로고
    • Microscale nonreductive release of O-linked glycans for subsequent analysis through MALDI mass spectrometry and capillary electrophoresis
    • DOI 10.1021/ac015534c
    • Y. Huang, Y. Mechref, and M.V. Novotny Microscale nonreductive release of O-linked glycans for subsequent analysis through MALDI mass spectrometry and capillary electrophoresis Anal. Chem. 73 2001 6063 6069 (Pubitemid 34042226)
    • (2001) Analytical Chemistry , vol.73 , Issue.24 , pp. 6063-6069
    • Huang, Y.1    Mechref, Y.2    Novotny, M.V.3
  • 22
    • 0037297818 scopus 로고    scopus 로고
    • Microscale analysis of mucin-type O-glycans by a coordinated fluorophore-assisted carbohydrate electrophoresis and mass spectrometry approach
    • DOI 10.1002/elps.200390071
    • C. Robbe, C. Capon, C. Flahaut, and J.-C. Michalski Microscale analysis of mucin-type O-glycans by a coordinated fluorophore-assisted carbohydrate electrophoresis and mass spectrometry approach Electrophoresis 24 2003 611 621 (Pubitemid 36336382)
    • (2003) Electrophoresis , vol.24 , Issue.4 , pp. 611-621
    • Robbe, C.1    Capon, C.2    Flahaut, C.3    Michalski, J.-C.4
  • 23
    • 0035983383 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry compatible β-elimination of O-linked oligosaccharides
    • DOI 10.1002/rcm.701
    • Y. Huang, Y. Konse, Y. Mechref, and M.V. Novotny Matrix-assisted laser desorption/ionization mass spectrometry compatible β-elimination of O-linked oligosaccharides Rapid Commun. Mass Spectrom. 16 2002 1199 1204 (Pubitemid 34619582)
    • (2002) Rapid Communications in Mass Spectrometry , vol.16 , Issue.12 , pp. 1199-1204
    • Huang, Y.1    Konse, T.2    Mechref, Y.3    Novotny, M.V.4
  • 24
    • 0035282989 scopus 로고    scopus 로고
    • Glycoprotein identification and localization of O-glycosylation sites by mass spectrometric analysis of deglycosylated/alkylaminylated peptide fragments
    • DOI 10.1006/abio.2000.4955
    • F. Hanisch, M. Jovanovic, and J. Peter-Katalinic Glycoprotein identification and localization of O-glycosylation sites by mass spectrometric analysis of deglycosylated/alkylaminylated peptide fragments Anal. Biochem. 290 2001 47 59 (Pubitemid 32182269)
    • (2001) Analytical Biochemistry , vol.290 , Issue.1 , pp. 47-59
    • Hanisch, F.-G.1    Jovanovic, M.2    Peter-Katalinic, J.3
  • 25
    • 0030883428 scopus 로고    scopus 로고
    • Nonreductive release of O-linked oligosaccharides from mucin glycoproteins for structure/function assignments as neoglycolipids: Application in the detection of novel ligands for E-selectin
    • DOI 10.1093/glycob/7.6.861
    • W. Chai, T. Feizi, C.T. Yuen, and A.M. Lawson Nonreductive release of O-linked oligosaccharides from mucin glycoproteins for structure/function assignments as neoglycolipids: application in the detection of novel ligands for E-selectin Glycobiology 7 1997 861 872 (Pubitemid 27385384)
    • (1997) Glycobiology , vol.7 , Issue.6 , pp. 861-872
    • Chai, W.1    Feizi, T.2    Yuen, C.-T.3    Lawson, A.M.4
  • 26
    • 0026801605 scopus 로고
    • Novel sulfated ligands for the cell adhesion molecule E-selectin revealed by the neoglycolipid technology among O-linked oligosaccharides on an ovarian cystadenoma glycoprotein
    • C.T. Yuen, A.M. Lawson, W. Chai, M. Larkin, M.S. Stoll, A.C. Stuart, F.X. Sullivan, T.J. Ahern, and T. Feizi Novel sulfated ligands for the cell adhesion molecule E-selectin revealed by the neoglycolipid technology among O-linked oligosaccharides on an ovarian cystadenoma glycoprotein Biochemistry 31 1992 9126 9131
    • (1992) Biochemistry , vol.31 , pp. 9126-9131
    • Yuen, C.T.1    Lawson, A.M.2    Chai, W.3    Larkin, M.4    Stoll, M.S.5    Stuart, A.C.6    Sullivan, F.X.7    Ahern, T.J.8    Feizi, T.9
  • 27
    • 77949858337 scopus 로고    scopus 로고
    • Rapid de-O-glycosylation concomitant with peptide labeling using microwave radiation and an alkyl amine base
    • S. Maniatis, H. Zhou, and V. Reinhold Rapid de-O-glycosylation concomitant with peptide labeling using microwave radiation and an alkyl amine base Anal. Chem. 82 2010 2421 2425
    • (2010) Anal. Chem. , vol.82 , pp. 2421-2425
    • Maniatis, S.1    Zhou, H.2    Reinhold, V.3
  • 28
    • 0035866603 scopus 로고    scopus 로고
    • Mass spectrometric determination of O-glycosylation sites using β-elimination and partial acid hydrolysis
    • DOI 10.1021/ac001288d
    • E. Mirgorodskaya, H. Hassan, H. Clausen, and P. Roepstorff Mass spectrometric determination of O-glycosylation sites using β-elimination and partial acid hydrolysis Anal. Chem. 73 2001 1263 1269 (Pubitemid 32861914)
    • (2001) Analytical Chemistry , vol.73 , Issue.6 , pp. 1263-1269
    • Mirgorodskaya, E.1    Hassan, H.2    Clausen, H.3    Roepstorff, P.4
  • 30
    • 0036570965 scopus 로고    scopus 로고
    • Recovery of intact 2-aminobenzamide-labeled O-glycans released from glycoproteins by hydrazinolysis
    • DOI 10.1006/abio.2002.5620
    • A.H. Merry, D.C.A. Neville, L. Royle, B. Mattews, D.J. Harvey, R.A. Dwek, and P.M. Rudd Recovery of intact 2-aminobenzamide-labeled O-glycans released from glycoproteins by hydrazinolysis Anal. Biochem. 304 2002 91 99 (Pubitemid 34492846)
    • (2002) Analytical Biochemistry , vol.304 , Issue.1 , pp. 91-99
    • Merry, A.H.1    Neville, D.C.A.2    Royle, L.3    Matthews, B.4    Harvey, D.J.5    Dwek, R.A.6    Rudd, P.M.7
  • 31
    • 0036571275 scopus 로고    scopus 로고
    • An analytical and structural database provides a strategy for sequencing O-glycans from microgram quantities of glycoproteins
    • DOI 10.1006/abio.2002.5619
    • L. Royle, T.S. Mattu, E. Hart, J.I. Langridge, A.H. Merry, N. Murphy, D.J. Harvey, R.A. Dwek, and P.M. Rudd An analytical and structural database provides a strategy for sequencing O-glycans from microgram quantities of glycoproteins Anal. Biochem. 304 2002 70 90 (Pubitemid 34492845)
    • (2002) Analytical Biochemistry , vol.304 , Issue.1 , pp. 70-90
    • Royle, L.1    Mattu, T.S.2    Hart, E.3    Langridge, J.I.4    Merry, A.H.5    Murphy, N.6    Harvey, D.J.7    Dwek, R.A.8    Rudd, P.M.9
  • 32
    • 0027441378 scopus 로고
    • Use of hydrazine to release in intact and unreduced form both N- and O- linked oligosaccharides from glycoproteins
    • DOI 10.1021/bi00053a037
    • T. Patel, J. Bruce, A. Merry, C. Bigge, M. Wormald, A. Jaques, and R. Parekh Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins Biochemistry 32 1993 679 693 (Pubitemid 23034909)
    • (1993) Biochemistry , vol.32 , Issue.2 , pp. 679-693
    • Patel, T.1    Bruce, J.2    Merry, A.3    Bigge, C.4    Wormald, M.5    Jaques, A.6    Parekh, R.7
  • 33
    • 0020020233 scopus 로고
    • Hydrazinolysis of asparagine-linked sugar chains to produce free oligosaccharides
    • S. Takasaki, T. Mizuochi, and A. Kobata Hydrazinolysis of asparagine-linked sugar chains to produce free oligosaccharides Methods Enzymol. 83 1982 263 268
    • (1982) Methods Enzymol. , vol.83 , pp. 263-268
    • Takasaki, S.1    Mizuochi, T.2    Kobata, A.3
  • 34
    • 0026659121 scopus 로고
    • Release of O-linked sugar chains from glycoproteins with anhydrous hydrazine and pyridylamination of the sugar chains with improved reaction conditions
    • N. Kuraya, and S. Hase Release of O-linked sugar chains from glycoproteins with anhydrous hydrazine and pyridylamination of the sugar chains with improved reaction conditions J. Biochem. 112 1992 122 126
    • (1992) J. Biochem. , vol.112 , pp. 122-126
    • Kuraya, N.1    Hase, S.2
  • 35
    • 46049104398 scopus 로고    scopus 로고
    • Application of the 50% hydrazine solution method for O-glycans release, their chemical labeling, and HPLC separation
    • DOI 10.1080/15376510701623755, PII 794365512
    • D.G. Kisiel, I. Radziejewska, and A. Gindienski Application of the 50% hydrazine solution method for O-glycans release, their chemical labeling, and HPLC separation Toxicol. Mech. Methods 18 2008 503 507 (Pubitemid 351896776)
    • (2008) Toxicology Mechanisms and Methods , vol.18 , Issue.6 , pp. 503-507
    • Kisiel, D.G.1    Radziejewska, I.2    Gindzienski, A.3
  • 36
    • 0028111344 scopus 로고
    • The elimination of O-linked glycans from glycoproteins under non-reducing conditions
    • DOI 10.1007/BF00731156
    • C.A. Coper, N.H. Packer, and J.W. Redmond The elimination of O-linked glycans from glycoproteins under non-reducing conditions Glycoconjugate J. 11 1994 163 167 (Pubitemid 24257181)
    • (1994) Glycoconjugate Journal , vol.11 , Issue.2 , pp. 163-167
    • Cooper, C.A.1    Packer, N.H.2    Redmond, J.W.3
  • 38
    • 0037967848 scopus 로고    scopus 로고
    • Sample clean-up method for analysis of complex-type N-glycans released from glycopeptides
    • DOI 10.1016/S0021-9673(03)00926-9
    • M. Nakano, K. Kakehi, and Y.C. Lee Sample clean-up method for analysis of complex-type N-glycans released from glycopeptides J. Chromatogr. A 1005 2003 13 21 (Pubitemid 36830969)
    • (2003) Journal of Chromatography A , vol.1005 , Issue.1-2 , pp. 13-21
    • Nakano, M.1    Kakehi, K.2    Lee, Y.C.3
  • 40
    • 0035056003 scopus 로고    scopus 로고
    • Anti-TNFα therapy of rheumatoid arthritis: What have we learned?
    • DOI 10.1146/annurev.immunol.19.1.163
    • M. Feldmann, and R.N. Maini Anti-TNFα therapy of rheumatoid arthritis: what have we learned? Ann. Rev Immunol. 19 2001 163 196 (Pubitemid 32368033)
    • (2001) Annual Review of Immunology , vol.19 , pp. 163-196
    • Feldmann, M.1    Maini, R.N.2
  • 41
    • 0027198002 scopus 로고
    • Soluble tumor necrosis factor (TNF) receptors are effective therapeutic agents in lethal endotoxemia and function simultaneously as both TNF carriers and TNF antagonists
    • K.M. Mohler, D.S. Torrance, C.A. Smith, R.G. Goodwin, K.E. Stremler, V.P. Fung, H. Madani, and M.B. Widmer Soluble tumor necrosis factor (TNF) receptors are effective therapeutic agents in lethal endotoxemia and function simultaneously as both TNF carriers and TNF antagonists J. Immunol. 151 1993 1548 1561 (Pubitemid 23219293)
    • (1993) Journal of Immunology , vol.151 , Issue.3 , pp. 1548-1561
    • Mohler, K.M.1    Torrance, D.S.2    Smith, C.A.3    Goodwin, R.G.4    Stremler, K.E.5    Fung, V.P.6    Madani, H.7    Widmer, M.B.8
  • 42
    • 0032731855 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer
    • E. Mirgorodskaya, P. Roepstorff, and R.A. Zubarev Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer Anal. Chem. 71 1999 4431 4436
    • (1999) Anal. Chem. , vol.71 , pp. 4431-4436
    • Mirgorodskaya, E.1    Roepstorff, P.2    Zubarev, R.A.3
  • 43
    • 0026701391 scopus 로고
    • Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue
    • H. Nishimura, T. Takao, S. Hase, Y. Shimonish, and S. Iwanaga Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue J. Biol Chem. 267 1992 17520 17525
    • (1992) J. Biol Chem. , vol.267 , pp. 17520-17525
    • Nishimura, H.1    Takao, T.2    Hase, S.3    Shimonish, Y.4    Iwanaga, S.5
  • 44
    • 77954506026 scopus 로고    scopus 로고
    • Role of glycans and glycosyltransferases in the regulation of Notch signaling
    • H. Jafar-Nejad, J. Leonardi, and R. Fernandez-Valdivia Role of glycans and glycosyltransferases in the regulation of Notch signaling Glycobiology 20 2010 931 949
    • (2010) Glycobiology , vol.20 , pp. 931-949
    • Jafar-Nejad, H.1    Leonardi, J.2    Fernandez-Valdivia, R.3
  • 45
    • 0032509527 scopus 로고    scopus 로고
    • Demonstration of the immature glycosaminoglycan tetrasaccharide sequence GlcAβ1-3Galβ1-3Galβ1-4Xyl on recombinant soluble human α-thrombomodulin: A possible mechanism generating "part-time" proteoglycans
    • S. Nadanaka, H. Kitagawa, and K. Sugahara Demonstration of the immature glycosaminoglycan tetrasaccharide sequence GlcAβ1-3Galβ1-3Galβ1- 4Xyl on recombinant soluble human α-thrombomodulin: a possible mechanism generating "part-time" proteoglycans J. Biol. Chem. 273 1998 33728 33734
    • (1998) J. Biol. Chem. , vol.273 , pp. 33728-33734
    • Nadanaka, S.1    Kitagawa, H.2    Sugahara, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.