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Volumn 382, Issue 1-2, 2012, Pages 167-176

Quantitative glycan profiling of normal human plasma derived immunoglobulin and its fragments Fab and Fc

Author keywords

2AA labeling; Fc Fab; Fluorescence detection; Glycan profile; Human IgG; IVIG

Indexed keywords

ANTHRANILIC ACID; CARBOHYDRATE; ENDOGLYCOSIDASE S; FC RECEPTOR; FUCOSE; GALACTOSE; GLYCAN; GLYCOSIDASE; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G; N ACETYLGLUCOSAMINE; PEPSIN A; PNGASE F; UNCLASSIFIED DRUG;

EID: 84863570384     PISSN: 00221759     EISSN: 18727905     Source Type: Journal    
DOI: 10.1016/j.jim.2012.05.022     Document Type: Article
Times cited : (71)

References (26)
  • 1
    • 74049141466 scopus 로고    scopus 로고
    • Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7microm sorbent
    • Ahn J., Bones J., Yu Y.Q., Rudd P.M., Gilar M. Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7microm sorbent. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2010, 878:403.
    • (2010) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.878 , pp. 403
    • Ahn, J.1    Bones, J.2    Yu, Y.Q.3    Rudd, P.M.4    Gilar, M.5
  • 3
    • 0027662451 scopus 로고
    • Endo β-N-acetylglucosaminidase F cleavage specificity with peptide free oligosaccharides
    • Anumula K.R. Endo β-N-acetylglucosaminidase F cleavage specificity with peptide free oligosaccharides. J. Mol. Recognit. 1993, 6:139.
    • (1993) J. Mol. Recognit. , vol.6 , pp. 139
    • Anumula, K.R.1
  • 4
    • 84861398695 scopus 로고    scopus 로고
    • New high-performance liquid chromatography assay for glycosyltransferases based on derivatization with anthranilic acid and fluorescence detection
    • Anumula K.R. New high-performance liquid chromatography assay for glycosyltransferases based on derivatization with anthranilic acid and fluorescence detection. Glycobiology 2012, 22:912.
    • (2012) Glycobiology , vol.22 , pp. 912
    • Anumula, K.R.1
  • 5
    • 0031820069 scopus 로고    scopus 로고
    • High resolution and high sensitivity methods for oligosaccharide mapping and characterization by normal phase high performance liquid chromatography following derivatization with highly fluorescent anthranilic acid
    • Anumula K.R., Dhume S.T. High resolution and high sensitivity methods for oligosaccharide mapping and characterization by normal phase high performance liquid chromatography following derivatization with highly fluorescent anthranilic acid. Glycobiology 1998, 8:685.
    • (1998) Glycobiology , vol.8 , pp. 685
    • Anumula, K.R.1    Dhume, S.T.2
  • 6
    • 0026027466 scopus 로고
    • Rapid characterization of asparagine linked oligosaccharides released from glycoproteins using a carbohydrate analyzer
    • Anumula K.R., Taylor P. Rapid characterization of asparagine linked oligosaccharides released from glycoproteins using a carbohydrate analyzer. Eur. J. Biochem. 1991, 195:269.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 269
    • Anumula, K.R.1    Taylor, P.2
  • 7
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold J.N., Wormald M.R., Sim R.B., Rudd P.M., Dwek R.A. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 2007, 25:21.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 8
    • 70350055478 scopus 로고    scopus 로고
    • Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I
    • Barb A.W., Brady E.K., Prestegard J.H. Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I. Biochemistry 2009, 48:9705.
    • (2009) Biochemistry , vol.48 , pp. 9705
    • Barb, A.W.1    Brady, E.K.2    Prestegard, J.H.3
  • 9
    • 0035875889 scopus 로고    scopus 로고
    • EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG
    • Collin M., Olsén A. EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG. EMBO J. 2001, 20:3046.
    • (2001) EMBO J. , vol.20 , pp. 3046
    • Collin, M.1    Olsén, A.2
  • 10
    • 0028829350 scopus 로고
    • Glycobiology: 'the function of sugar in the IgG molecule'
    • Dwek R.A., Lellouch A.C., Wormald M.R. Glycobiology: 'the function of sugar in the IgG molecule'. J. Anat. 1995, 187:279.
    • (1995) J. Anat. , vol.187 , pp. 279
    • Dwek, R.A.1    Lellouch, A.C.2    Wormald, M.R.3
  • 11
    • 82455171807 scopus 로고    scopus 로고
    • Rapid LC-MS screening for IgG Fc modifications and allelic variants in blood
    • Goetze A.M., Zhang Z., Liu L., Jacobsen F.W., Flynn G.C. Rapid LC-MS screening for IgG Fc modifications and allelic variants in blood. Mol. Immunol. 2011, 49:338.
    • (2011) Mol. Immunol. , vol.49 , pp. 338
    • Goetze, A.M.1    Zhang, Z.2    Liu, L.3    Jacobsen, F.W.4    Flynn, G.C.5
  • 12
    • 0030571019 scopus 로고    scopus 로고
    • A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles
    • Guile G.R., Rudd P.M., Wing D.R., Prime S.B., Dwek R.A. A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles. Anal. Biochem. 1996, 240:210.
    • (1996) Anal. Biochem. , vol.240 , pp. 210
    • Guile, G.R.1    Rudd, P.M.2    Wing, D.R.3    Prime, S.B.4    Dwek, R.A.5
  • 13
    • 33646093725 scopus 로고    scopus 로고
    • Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis
    • Holland M., Yagi H., Takahashi N., Kato K., Savage C.O., Goodall D.M., Jefferis R. Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis. Biochim. Biophys. Acta 2006, 1760:669.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 669
    • Holland, M.1    Yagi, H.2    Takahashi, N.3    Kato, K.4    Savage, C.O.5    Goodall, D.M.6    Jefferis, R.7
  • 14
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis R. Glycosylation of recombinant antibody therapeutics. Biotechnol. Prog. 2005, 21:11.
    • (2005) Biotechnol. Prog. , vol.21 , pp. 11
    • Jefferis, R.1
  • 15
    • 67649394336 scopus 로고    scopus 로고
    • Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action
    • (Review)
    • Jefferis R. Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action. Trends Pharmacol. Sci. 2009, 30:356. (Review).
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 356
    • Jefferis, R.1
  • 17
    • 40749147518 scopus 로고    scopus 로고
    • The N-linked sugar chains of human immunoglobulin G: their unique pattern, and their functional roles
    • Kobata A. The N-linked sugar chains of human immunoglobulin G: their unique pattern, and their functional roles. Biochim. Biophys. Acta 2008, 1780:472.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 472
    • Kobata, A.1
  • 19
    • 34548409568 scopus 로고    scopus 로고
    • Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry
    • Mimura Y., Ashton P.R., Takahashi N., Harvey D.J., Jefferis R. Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry. J. Immunol. Methods 2007, 326:116.
    • (2007) J. Immunol. Methods , vol.326 , pp. 116
    • Mimura, Y.1    Ashton, P.R.2    Takahashi, N.3    Harvey, D.J.4    Jefferis, R.5
  • 20
    • 0019934863 scopus 로고
    • Structural and numerical variations of the carbohydrate moiety of immunoglobulin G
    • Mizuochi T., Taniguchi T., Shimizu A., Kobata A. Structural and numerical variations of the carbohydrate moiety of immunoglobulin G. J. Immunol. 1982, 129:2016.
    • (1982) J. Immunol. , vol.129 , pp. 2016
    • Mizuochi, T.1    Taniguchi, T.2    Shimizu, A.3    Kobata, A.4
  • 21
    • 37549036732 scopus 로고    scopus 로고
    • Fc gamma receptors as regulators of immune responses
    • Nimmerjahn F., Ravetch J.V. Fc gamma receptors as regulators of immune responses. Nat. Rev. Immunol. 2008, 8:34.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 34
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 22
    • 0030043369 scopus 로고    scopus 로고
    • Porcine fibrinogen glycopeptides: substrates for detecting Endo β-N-acetylglucosaminidases F2 and F3
    • Plummer T.H., Phelan A.W., Tarentino A.L. Porcine fibrinogen glycopeptides: substrates for detecting Endo β-N-acetylglucosaminidases F2 and F3. Anal. Biochem. 1996, 235:98.
    • (1996) Anal. Biochem. , vol.235 , pp. 98
    • Plummer, T.H.1    Phelan, A.W.2    Tarentino, A.L.3
  • 23
    • 34548475063 scopus 로고    scopus 로고
    • Automated sample preparation facilitated by PhyNexus MEA purification system for oligosaccharide mapping of glycoproteins
    • Prater B.D., Anumula K.R., Hutchins J.T. Automated sample preparation facilitated by PhyNexus MEA purification system for oligosaccharide mapping of glycoproteins. Anal. Biochem. 2007, 369:202.
    • (2007) Anal. Biochem. , vol.369 , pp. 202
    • Prater, B.D.1    Anumula, K.R.2    Hutchins, J.T.3
  • 26
    • 0029962752 scopus 로고    scopus 로고
    • Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients
    • Youings A., Chang S.C., Dwek R.A., Scragg I.G. Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients. Biochem. J. 1996, 314:621.
    • (1996) Biochem. J. , vol.314 , pp. 621
    • Youings, A.1    Chang, S.C.2    Dwek, R.A.3    Scragg, I.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.