메뉴 건너뛰기




Volumn 49, Issue 27, 2010, Pages 5671-5682

Recognition of galactose-deficient O-glycans in the hinge region of IgA1 by N-acetylgalactosamine-specific snail lectins: A comparative binding study.

Author keywords

[No Author keywords available]

Indexed keywords

BINDING STUDIES; CELL LINES; DIAGNOSTIC TOOLS; GLYCOPEPTIDES; GLYCOSYLATED; HEALTHY CONTROLS; IMMUNE COMPLEX; INFLAMMATORY RESPONSE; KIDNEY DISEASE; LECTIN RECOGNITION; MESANGIAL CELLS; NEPHROPATHY; O-GLYCANS; PERIPHERAL BLOOD; SURFACE PLASMON RESONANCE SPECTROSCOPY;

EID: 77954692713     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi9019498     Document Type: Article
Times cited : (35)

References (64)
  • 1
    • 0034017259 scopus 로고    scopus 로고
    • Increased N-linked glycosylation leading to oversialylation of monomeric immunoglobulin A1 from patients with Sjögren's syndrome
    • Basset, C., Durand, V., Jamin, C., Clement, J., Pennec, Y., Youinou, P., Dueymes, M., and Roitt, I. M. (2000) Increased N-linked glycosylation leading to oversialylation of monomeric immunoglobulin A1 from patients with Sjögren's syndrome. Scand. J. Immunol. 51, 300-306.
    • (2000) Scand. J. Immunol. , vol.51 , pp. 300-306
    • Basset, C.1    Durand, V.2    Jamin, C.3    Clement, J.4    Pennec, Y.5    Youinou, P.6    Dueymes, M.7    Roitt, I.M.8
  • 4
    • 0030666267 scopus 로고    scopus 로고
    • Alterations in the O-linked glycosylation of IgA1 in children with Henoch-Schönlein purpura
    • Saulsbury, F. T. (1997) Alterations in the O-linked glycosylation of IgA1 in children with Henoch-Schönlein purpura. J. Rheumatol. 24, 2246-2249.
    • (1997) J. Rheumatol. , vol.24 , pp. 2246-2249
    • Saulsbury, F.T.1
  • 5
    • 0027355459 scopus 로고
    • Defective galactosylation and clearance of IgA1 molecules as a possible etiopathogenic factor in IgA nephropathy
    • Mestecky, J., Tomana, M., Crowley-Nowick, P. A., Moldoveanu, Z., Julian, B. A., and Jackson, S. (1993) Defective galactosylation and clearance of IgA1 molecules as a possible etiopathogenic factor in IgA nephropathy. Contrib. Nephrol. 104, 172-182.
    • (1993) Contrib. Nephrol. , vol.104 , pp. 172-182
    • Mestecky, J.1    Tomana, M.2    Crowley-Nowick, P.A.3    Moldoveanu, Z.4    Julian, B.A.5    Jackson, S.6
  • 6
    • 0029001438 scopus 로고
    • Galactosylation of N- and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathy
    • Allen, A. C., Harper, S. J., and Feehally, J. (1995) Galactosylation of N- and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathy. Clin. Exp. Immunol. 100, 470-474.
    • (1995) Clin. Exp. Immunol. , vol.100 , pp. 470-474
    • Allen, A.C.1    Harper, S.J.2    Feehally, J.3
  • 7
    • 0030836018 scopus 로고    scopus 로고
    • Galactose-deficient IgA1 in sera of IgA nephropathy patients is present in complexes with IgG
    • Tomana, M., Matousovic, K., Julian, B. A., Radl, J., Konecny, K., and Mestecky, J. (1997) Galactose-deficient IgA1 in sera of IgA nephropathy patients is present in complexes with IgG. Kidney Int. 52, 509-516.
    • (1997) Kidney Int. , vol.52 , pp. 509-516
    • Tomana, M.1    Matousovic, K.2    Julian, B.A.3    Radl, J.4    Konecny, K.5    Mestecky, J.6
  • 8
    • 0032695357 scopus 로고    scopus 로고
    • Circulating immune complexes in IgA nephropathy consist of IgA1 with galactose-deficient hinge region and antiglycan antibodies
    • Tomana, M., Novak, J., Julian, B. A., Matousovic, K., Konecny, K., and Mestecky, J. (1999) Circulating immune complexes in IgA nephropathy consist of IgA1 with galactose-deficient hinge region and antiglycan antibodies. J. Clin. Invest. 104, 73-81.
    • (1999) J. Clin. Invest. , vol.104 , pp. 73-81
    • Tomana, M.1    Novak, J.2    Julian, B.A.3    Matousovic, K.4    Konecny, K.5    Mestecky, J.6
  • 11
    • 0031925983 scopus 로고    scopus 로고
    • Abnormal IgA glycosylation in Henoch-Schönlein purpura restricted to patients with clinical nephritis
    • Allen, A. C., Willis, F. R., Beattie, T. J., and Feehally, J. (1998) Abnormal IgA glycosylation in Henoch-Schönlein purpura restricted to patients with clinical nephritis. Nephrol., Dial., Transplant. 13, 930-934.
    • (1998) Nephrol., Dial., Transplant. , vol.13 , pp. 930-934
    • Allen, A.C.1    Willis, F.R.2    Beattie, T.J.3    Feehally, J.4
  • 12
    • 0030614706 scopus 로고    scopus 로고
    • Henoch-Schönlein purpura with immunoglobulin A nephropathy and abnormalities of immunoglobulin A in a Wiskott-Aldrich syndrome carrier
    • Lasseur, C., Allen, A. C., Deminiere, C., Aparicio, M., Feehally, J., and Combe, C. (1997) Henoch-Schönlein purpura with immunoglobulin A nephropathy and abnormalities of immunoglobulin A in a Wiskott-Aldrich syndrome carrier. Am. J. Kidney Dis. 29, 285-287.
    • (1997) Am. J. Kidney Dis. , vol.29 , pp. 285-287
    • Lasseur, C.1    Allen, A.C.2    Deminiere, C.3    Aparicio, M.4    Feehally, J.5    Combe, C.6
  • 13
    • 0016293141 scopus 로고
    • Structure of the carbohydrate units of IgA1 immunoglobulin. I. Composition, glycopeptide isolation, and structure of the asparagine-linked oligosaccharide units
    • Baenziger, J., and Kornfeld, S. (1974) Structure of the carbohydrate units of IgA1 immunoglobulin. I. Composition, glycopeptide isolation, and structure of the asparagine-linked oligosaccharide units. J. Biol. Chem. 249, 7260-7269.
    • (1974) J. Biol. Chem. , Issue.249 , pp. 7260-7269
    • Baenziger, J.1    Kornfeld, S.2
  • 14
    • 0016270014 scopus 로고
    • Structure of the carbohydrate units of IgA1 immunoglobulin. II. Structure of the O-glycosidically linked oligosaccharide units
    • Baenziger, J., and Kornfeld, S. (1974) Structure of the carbohydrate units of IgA1 immunoglobulin. II. Structure of the O-glycosidically linked oligosaccharide units. J. Biol. Chem. 249, 7270-7281.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7270-7281
    • Baenziger, J.1    Kornfeld, S.2
  • 15
    • 0017240387 scopus 로고
    • The differences in carbohydrate composition between the subclasses of IgA immunoglobulins
    • Tomana, M., Niedermeier, W., Mestecky, J., and Skvaril, F. (1976) The differences in carbohydrate composition between the subclasses of IgA immunoglobulins. Immunochemistry 13, 325-328.
    • (1976) Immunochemistry , vol.13 , pp. 325-328
    • Tomana, M.1    Niedermeier, W.2    Mestecky, J.3    Skvaril, F.4
  • 16
    • 0010430522 scopus 로고
    • Location and structural significance of the oligosaccharides in human Ig-A1 and IgA2 immunoglobulins
    • Torano, A., Tsuzukida, Y., Liu, Y. S., and Putnam, F. W. (1977) Location and structural significance of the oligosaccharides in human Ig-A1 and IgA2 immunoglobulins. Proc. Natl. Acad. Sci. U.S.A. 74, 2301-2305.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 2301-2305
    • Torano, A.1    Tsuzukida, Y.2    Liu, Y.S.3    Putnam, F.W.4
  • 17
    • 0017160906 scopus 로고
    • Complete covalent structure of a human IgA1 immunoglobulin
    • Liu, Y.-S. V., Low, T. L. K., Infante, A., and Putnam, F. W. (1976) Complete covalent structure of a human IgA1 immunoglobulin. Science 193, 1017-1019.
    • (1976) Science , vol.193 , pp. 1017-1019
    • Liu, Y.-S.V.1    Low, T.L.K.2    Infante, A.3    Putnam, F.W.4
  • 18
    • 54849437907 scopus 로고    scopus 로고
    • Analysis of IgA1 N-glycosylation and its contribution to FcRRI binding
    • Gomes, M. M., Wall, S. B., Takahashi, K., Novak, J., Renfrow, M. B., and Herr, A. B. (2008) Analysis of IgA1 N-glycosylation and its contribution to FcRRI binding. Biochemistry 47, 11285-11299.
    • (2008) Biochemistry , vol.47 , pp. 11285-11299
    • Gomes, M.M.1    Wall, S.B.2    Takahashi, K.3    Novak, J.4    Renfrow, M.B.5    Herr, A.B.6
  • 19
    • 0015459784 scopus 로고
    • Partial duplication in the "hinge" region of IgA 1 myeloma proteins
    • Frangione, B., and Wolfenstein-Todel, C. (1972) Partial duplication in the "hinge" region of IgA 1 myeloma proteins. Proc. Natl. Acad. Sci. U.S.A. 69, 3673-3676.
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 3673-3676
    • Frangione, B.1    Wolfenstein-Todel, C.2
  • 20
    • 0024841285 scopus 로고
    • O-linked oligosaccharides from human serum immunoglobulin A1
    • Field, M. C., Dwek, R. A., Edge, C. J., and Rademacher, T. W. (1989) O-linked oligosaccharides from human serum immunoglobulin A1. Biochem. Soc. Trans. 17, 1034-1035.
    • (1989) Biochem. Soc. Trans. , vol.17 , pp. 1034-1035
    • Field, M.C.1    Dwek, R.A.2    Edge, C.J.3    Rademacher, T.W.4
  • 21
    • 0029681114 scopus 로고    scopus 로고
    • Estimation of the number of O-linked oligosaccharides per heavy chain of human serum IgA1 by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS) analysis of the hinge glycopeptide
    • Iwase, H., Tanaka, A., Hiki, Y., Kokubo, T., Ishii-Karakasa, I., Kobayashi, Y., and Hotta, K. (1996) Estimation of the number of O-linked oligosaccharides per heavy chain of human serum IgA1 by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS) analysis of the hinge glycopeptide. J. Biochem. 120, 393-397.
    • (1996) J. Biochem. , vol.120 , pp. 393-397
    • Iwase, H.1    Tanaka, A.2    Hiki, Y.3    Kokubo, T.4    Ishii-Karakasa, I.5    Kobayashi, Y.6    Hotta, K.7
  • 22
    • 0031915973 scopus 로고    scopus 로고
    • The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on FcR receptor interactions
    • Mattu, T. S., Pleass, R. J., Willis, A. C., Kilian, M., Wormald, M. R., Lellouch, A. C., Rudd, P. M., Woof, J. M., and Dwek, R. A. (1998) The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on FcR receptor interactions. J. Biol. Chem. 273, 2260-2272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2260-2272
    • Mattu, T.S.1    Pleass, R.J.2    Willis, A.C.3    Kilian, M.4    Wormald, M.R.5    Lellouch, A.C.6    Rudd, P.M.7    Woof, J.M.8    Dwek, R.A.9
  • 24
    • 21444448470 scopus 로고    scopus 로고
    • Determination of aberrant O-glycosylation in the IgA1 hinge region by electron capture dissociation Fourier transform-ion cyclotron resonance mass spectrometry
    • Renfrow, M. B., Cooper, H. J., Tomana, M., Kulhavy, R., Hiki, Y., Toma, K.,Emmett, M. R., Mestecky, J., Marshall, A. G., and Novak, J. (2005) Determination of aberrant O-glycosylation in the IgA1 hinge region by electron capture dissociation Fourier transform-ion cyclotron resonance mass spectrometry. J. Biol. Chem. 280, 19136-19145.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19136-19145
    • Renfrow, M.B.1    Cooper, H.J.2    Tomana, M.3    Kulhavy, R.4    Hiki, Y.5    Toma K.Emmett, M.R.6    Mestecky, J.7    Marshall, A.G.8    Novak, J.9
  • 25
    • 4444307298 scopus 로고    scopus 로고
    • Human serum IgA1 is substituted with up to six O-glycans as shown by matrix assisted laser desorption ionisation time-of-flight mass spectrometry
    • Tarelli, E., Smith, A. C., Hendry, B. M., Challacombe, S. J., and Pouria, S. (2004) Human serum IgA1 is substituted with up to six O-glycans as shown by matrix assisted laser desorption ionisation time-of-flight mass spectrometry. Carbohydr. Res. 339, 2329-2335.
    • (2004) Carbohydr. Res. , vol.339 , pp. 2329-2335
    • Tarelli, E.1    Smith, A.C.2    Hendry, B.M.3    Challacombe, S.J.4    Pouria, S.5
  • 26
    • 35648929345 scopus 로고    scopus 로고
    • Analysis of O-glycan heterogeneity in IgA1 myeloma proteins by Fourier transform ion cyclotron resonance mass spectrometry: Implications for IgA nephropathy
    • Renfrow, M. B., Mackay, C. L., Chalmers, M. J., Julian, B. A., Mestecky, J., Kilian, M., Poulsen, K., Emmett, M. R., Marshall, A. G., and Novak, J. (2007) Analysis of O-glycan heterogeneity in IgA1 myeloma proteins by Fourier transform ion cyclotron resonance mass spectrometry: Implications for IgA nephropathy. Anal. Bioanal. Chem. 389, 1397-1407.
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 1397-1407
    • Renfrow, M.B.1    Mackay, C.L.2    Chalmers, M.J.3    Julian, B.A.4    Mestecky, J.5    Kilian, M.6    Poulsen, K.7    Emmett, M.R.8    Marshall, A.G.9    Novak, J.10
  • 27
    • 0028280439 scopus 로고
    • Structural analysis of the N-glycans from human immunoglobulin A1: Comparison of normal human serum immunoglobulin A1 with that isolated from patients with rheumatoid arthritis
    • Field, M. C., Amatayakul-Chantler, S., Rademacher, T. W., Rudd, P. M., and Dwek, R. A. (1994) Structural analysis of the N-glycans from human immunoglobulin A1: Comparison of normal human serum immunoglobulin A1 with that isolated from patients with rheumatoid arthritis. Biochem. J. 299 (Part 1), 261-275.
    • (1994) Biochem. J. , vol.299 , Issue.PART. 1 , pp. 261-275
    • Field, M.C.1    Amatayakul-Chantler, S.2    Rademacher, T.W.3    Rudd, P.M.4    Dwek, R.A.5
  • 28
    • 0035723058 scopus 로고    scopus 로고
    • Mesangial IgA1 in IgA nephropathy exhibits aberrant O-glycosylation: Observations in three patients
    • Allen, A. C., Bailey, E. M., Brenchley, P. E., Buck, K. S., Barratt, J., and Feehally, J. (2001) Mesangial IgA1 in IgA nephropathy exhibits aberrant O-glycosylation: Observations in three patients. Kidney Int. 60, 969-973.
    • (2001) Kidney Int. , vol.60 , pp. 969-973
    • Allen, A.C.1    Bailey, E.M.2    Brenchley, P.E.3    Buck, K.S.4    Barratt, J.5    Feehally, J.6
  • 29
    • 0029204973 scopus 로고
    • O-linked oligosaccharide on IgA1 hinge region in IgA nephropathy. Fundamental study for precise structure and possible role
    • Hiki, Y., Horii, A., Iwase, H., Tanaka, A., Toda, Y., Hotta, K., and Kobayashi, Y. (1995) O-linked oligosaccharide on IgA1 hinge region in IgA nephropathy. Fundamental study for precise structure and possible role. Contrib. Nephrol. 111, 73-84.
    • (1995) Contrib. Nephrol. , vol.111 , pp. 73-84
    • Hiki, Y.1    Horii, A.2    Iwase, H.3    Tanaka, A.4    Toda, Y.5    Hotta, K.6    Kobayashi, Y.7
  • 30
    • 0034753207 scopus 로고    scopus 로고
    • Progress in molecular and genetic studies of IgA nephropathy
    • Novak, J., Julian, B. A., Tomana, M., and Mestecky, J. (2001) Progress in molecular and genetic studies of IgA nephropathy. J. Clin. Immunol. 21, 310-327.
    • (2001) J. Clin. Immunol. , vol.21 , pp. 310-327
    • Novak, J.1    Julian, B.A.2    Tomana, M.3    Mestecky, J.4
  • 32
    • 0038688385 scopus 로고    scopus 로고
    • New insights into the pathogenesis of IgA nephropathy. Pathogenesis of IgA nephropathy
    • Smith, A. C., and Feehally, J. (2003) New insights into the pathogenesis of IgA nephropathy. Pathogenesis of IgA nephropathy. Springer Semin. Immunopathol. 24, 477-493.
    • (2003) Springer Semin. Immunopathol. , vol.24 , pp. 477-493
    • Smith, A.C.1    Feehally, J.2
  • 36
    • 33645103579 scopus 로고    scopus 로고
    • Self-aggregated deglycosylated IgA1 with or without IgG were associated with the development of IgA nephropathy
    • Yan, Y., Xu, L. X., Zhang, J. J., Zhang, Y., and Zhao, M. H. (2006) Self-aggregated deglycosylated IgA1 with or without IgG were associated with the development of IgA nephropathy. Clin. Exp. Immunol. 144, 17-24.
    • (2006) Clin. Exp. Immunol. , vol.144 , pp. 17-24
    • Yan, Y.1    Xu, L.X.2    Zhang, J.J.3    Zhang, Y.4    Zhao, M.H.5
  • 39
    • 0028147981 scopus 로고
    • Glycosylation of IgA is required for optimal activation of the alternative complement pathway by immune complexes
    • Zhang, W., and Lachmann, P. J. (1994) Glycosylation of IgA is required for optimal activation of the alternative complement pathway by immune complexes. Immunology 81, 137-141.
    • (1994) Immunology , vol.81 , pp. 137-141
    • Zhang, W.1    Lachmann, P.J.2
  • 42
    • 0028872958 scopus 로고
    • Use of lectins as diagnostic and therapeutic tools for cancer
    • Mody, R., Joshi, S., and Chaney, W. (1995) Use of lectins as diagnostic and therapeutic tools for cancer. J. Pharmacol. Toxicol. Methods 33, 1-10.
    • (1995) J. Pharmacol. Toxicol. Methods , vol.33 , pp. 1-10
    • Mody, R.1    Joshi, S.2    Chaney, W.3
  • 43
    • 0033977912 scopus 로고    scopus 로고
    • The involvement of Helix pomatia lectin (HPA) binding N-acetylgalactosamine glycans in cancer progression
    • Brooks, S. A. (2000) The involvement of Helix pomatia lectin (HPA) binding N-acetylgalactosamine glycans in cancer progression. Histol. Histopathol. 15, 143-158.
    • (2000) Histol. Histopathol. , vol.15 , pp. 143-158
    • Brooks, S.A.1
  • 44
    • 77956671151 scopus 로고    scopus 로고
    • (Schachter, H., Ed.), Elsevier, New York
    • Tomana, M. (1996) in Glycoproteins and Disease (Schachter, H., Ed.) pp 291-298, Elsevier, New York.
    • (1996) Glycoproteins and Disease , pp. 291-298
    • Tomana, M.1
  • 45
    • 0028981441 scopus 로고
    • Glycoforms of serum R1-acid glycoprotein as markers of inflammation and cancer
    • Mackiewicz, A., and Mackiewicz, K. (1995) Glycoforms of serum R1-acid glycoprotein as markers of inflammation and cancer. Glycoconjugate J. 12, 241-247.
    • (1995) Glycoconjugate J. , vol.12 , pp. 241-247
    • Mackiewicz, A.1    Mackiewicz, K.2
  • 46
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannosebinding protein
    • Malhotra, R., Wormald, M. R., Rudd, P. M., Fischer, P. B., Dwek, R. A., and Sim, R. B. (1995) Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannosebinding protein. Nat. Med. 1, 237-243.
    • (1995) Nat. Med. , vol.1 , pp. 237-243
    • Malhotra, R.1    Wormald, M.R.2    Rudd, P.M.3    Fischer, P.B.4    Dwek, R.A.5    Sim, R.B.6
  • 47
    • 0034976643 scopus 로고    scopus 로고
    • Time course of endothelial cell proliferation and microvascular remodeling in chronic inflammation
    • Ezaki, T., Baluk, P., Thurston, G., La Barbara, A., Woo, C., and McDonald, D. M. (2001) Time course of endothelial cell proliferation and microvascular remodeling in chronic inflammation. Am. J. Pathol. 158, 2043-2055.
    • (2001) Am. J. Pathol. , vol.158 , pp. 2043-2055
    • Ezaki, T.1    Baluk, P.2    Thurston, G.3    La Barbara, A.4    Woo, C.5    McDonald, D.M.6
  • 53
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78, 1606-1619.
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 55
    • 0037470618 scopus 로고    scopus 로고
    • Bivalent binding of IgA1 to FcRRI suggests a mechanism for cytokine activation of IgA phagocytosis
    • Herr, A. B., White, C. L., Milburn, C., Wu, C., and Bjorkman, P. J. (2003) Bivalent binding of IgA1 to FcRRI suggests a mechanism for cytokine activation of IgA phagocytosis. J. Mol. Biol. 327, 645-657.
    • (2003) J. Mol. Biol. , vol.327 , pp. 645-657
    • Herr, A.B.1    White, C.L.2    Milburn, C.3    Wu, C.4    Bjorkman, P.J.5
  • 56
    • 0001452803 scopus 로고    scopus 로고
    • Heparin-induced self-association of fibroblast growth factor-2. Evidence for two oligomerization processes
    • Herr, A. B., Ornitz, D. M., Sasisekharan, R., Venkataraman, G., and Waksman, G. (1997) Heparin-induced self-association of fibroblast growth factor-2. Evidence for two oligomerization processes. J. Biol. Chem. 272, 16382-16389.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16382-16389
    • Herr, A.B.1    Ornitz, D.M.2    Sasisekharan, R.3    Venkataraman, G.4    Waksman, G.5
  • 57
    • 0025639888 scopus 로고
    • Impairment of jacalin binding to serum IgA in IgA nephropathy
    • Andre, P. M., Le Pogamp, P., and Chevet, D. (1990) Impairment of jacalin binding to serum IgA in IgA nephropathy. J. Clin. Lab. Anal. 4, 115-119.
    • (1990) J. Clin. Lab. Anal. , vol.4 , pp. 115-119
    • Andre, P.M.1    Le Pogamp, P.2    Chevet, D.3
  • 59
    • 0034442307 scopus 로고    scopus 로고
    • Affinity enhancement by multivalent lectin-carbohydrate interaction
    • Lee, R. T., and Lee, Y. C. (2000) Affinity enhancement by multivalent lectin-carbohydrate interaction. Glycoconjugate J. 17, 543-551.
    • (2000) Glycoconjugate J. , vol.17 , pp. 543-551
    • Lee, R.T.1    Lee, Y.C.2
  • 60
    • 29444435597 scopus 로고    scopus 로고
    • Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: Quantitative analysis by frontal affinity chromatography
    • Tachibana, K., Nakamura, S., Wang, H., Iwasaki, H., Maebara, K., Cheng, L., Hirabayashi, J., and Narimatsu, H. (2006) Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: Quantitative analysis by frontal affinity chromatography. Glycobiology 16, 46-53.
    • (2006) Glycobiology , vol.16 , pp. 46-53
    • Tachibana, K.1    Nakamura, S.2    Wang, H.3    Iwasaki, H.4    Maebara, K.5    Cheng, L.6    Hirabayashi, J.7    Narimatsu, H.8
  • 61
    • 0032840295 scopus 로고    scopus 로고
    • Analysis of IgA1 O-glycans in IgA nephropathy by fluorophore- assisted carbohydrate electrophoresis
    • Allen, A. C., Bailey, E. M., Barratt, J., Buck, K. S., and Feehally, J. (1999) Analysis of IgA1 O-glycans in IgA nephropathy by fluorophore- assisted carbohydrate electrophoresis. J. Am. Soc. Nephrol. 10, 1763-1771.
    • (1999) J. Am. Soc. Nephrol. , vol.10 , pp. 1763-1771
    • Allen, A.C.1    Bailey, E.M.2    Barratt, J.3    Buck, K.S.4    Feehally, J.5
  • 62
    • 0031944497 scopus 로고    scopus 로고
    • Analyses of IgA1 hinge glycopeptides in IgA nephropathy by matrix-assisted laser desorption/ionization timeof- flight mass spectrometry
    • Hiki, Y., Tanaka, A., Kokubo, T., Iwase, H., Nishikido, J., Hotta, K., and Kobayashi, Y. (1998) Analyses of IgA1 hinge glycopeptides in IgA nephropathy by matrix-assisted laser desorption/ionization timeof- flight mass spectrometry. J. Am. Soc. Nephrol. 9, 577-582.
    • (1998) J. Am. Soc. Nephrol. , vol.9 , pp. 577-582
    • Hiki, Y.1    Tanaka, A.2    Kokubo, T.3    Iwase, H.4    Nishikido, J.5    Hotta, K.6    Kobayashi, Y.7
  • 64
    • 0033548612 scopus 로고    scopus 로고
    • The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: A study by X-ray and neutron solution scattering and homology modelling
    • Boehm, M. K., Woof, J. M., Kerr, M. A., and Perkins, S. J. (1999) The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: A study by X-ray and neutron solution scattering and homology modelling. J. Mol. Biol. 286, 1421-1447.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1421-1447
    • Boehm, M.K.1    Woof, J.M.2    Kerr, M.A.3    Perkins, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.