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Volumn 9, Issue 11, 1999, Pages 1191-1197

Specialized expression of simple O-glycans along the rat kidney nephron

Author keywords

Amaranthin; Glycoprotein; Histochemistry; Kidney; O glycans

Indexed keywords

AMARANTH; GLYCAN; GLYCOPROTEIN; GLYCOSYLTRANSFERASE; LECTIN; MONOCLONAL ANTIBODY;

EID: 0032724904     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/9.11.1191     Document Type: Article
Times cited : (2)

References (60)
  • 1
    • 0030035111 scopus 로고    scopus 로고
    • cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. GalNAc-T3
    • Bennett,E.P., Hassan,H. and Clausen,H. (1996) cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. GalNAc-T3. J. Biol. Chem., 271, 17006-17012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17006-17012
    • Bennett, E.P.1    Hassan, H.2    Clausen, H.3
  • 2
    • 0027196404 scopus 로고
    • Clinical aspects of glycoprotein biosynthesis
    • Brockhausen,I. (1993) Clinical aspects of glycoprotein biosynthesis. Crit. Rev. Clin. Lab Sci., 30, 65-151.
    • (1993) Crit. Rev. Clin. Lab Sci. , vol.30 , pp. 65-151
    • Brockhausen, I.1
  • 3
    • 77957231504 scopus 로고
    • Biosynthesis of O-glycans of the N-acetylgalactosamine-α-Ser/Thr linkage type
    • Montreuil,J., Schachter,H. and Vliegenthart,J. (eds.), Elsevier Science, Amsterdam
    • Brockhausen,I. (1995) Biosynthesis of O-glycans of the N-acetylgalactosamine-α-Ser/Thr linkage type. In: Montreuil,J., Schachter,H. and Vliegenthart,J. (eds.), Glycoproteins. Elsevier Science, Amsterdam, pp. 201-259.
    • (1995) Glycoproteins , pp. 201-259
    • Brockhausen, I.1
  • 4
    • 0022035224 scopus 로고
    • Lectin-gold cytochemistry reveals intercalated cell heterogeneity along rat kidney collecting ducts
    • Brown,D., Roth,J. and Orci,L. (1985) Lectin-gold cytochemistry reveals intercalated cell heterogeneity along rat kidney collecting ducts. Am. J. Physiol., 248, C348-C356.
    • (1985) Am. J. Physiol. , vol.248
    • Brown, D.1    Roth, J.2    Orci, L.3
  • 5
    • 0031594236 scopus 로고    scopus 로고
    • Immunocytochemical localization of α2,3 (N)-sialyltransferase (ST3Gal III) in cell lines and rat kidney tissue sections: Evidence for Golgi and post-Golgi localization
    • Burger,P.C., Lötscher,M, Streiff,M., Kleene,R., Kaissling,B. and Berger,E.G. (1998) Immunocytochemical localization of α2,3 (N)-sialyltransferase (ST3Gal III) in cell lines and rat kidney tissue sections: evidence for Golgi and post-Golgi localization. Glycobiology, 8, 245-257.
    • (1998) Glycobiology , vol.8 , pp. 245-257
    • Burger, P.C.1    Lötscher, M.2    Streiff, M.3    Kleene, R.4    Kaissling, B.5    Berger, E.G.6
  • 6
    • 0029854393 scopus 로고    scopus 로고
    • A family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases control the initiation of mucin-type O-linked glycosylation
    • Clausen,H. and Bennett,E.P. (1996) A family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases control the initiation of mucin-type O-linked glycosylation. Glycobiology, 6, 635-646.
    • (1996) Glycobiology , vol.6 , pp. 635-646
    • Clausen, H.1    Bennett, E.P.2
  • 7
    • 0028823397 scopus 로고
    • Molecular cloning, expression, chromosomal assignment and tissue-specific expression of a murine α- (1,3)-fucosyltransferase locus corresponding to the human ELAM-1 ligand fucosyl transferase
    • Gersten,K.M., Natsuka,S., Trinchera,M., Petryniak,B., Kelly,R.J., Hiraiwa,N., Jenkins,N.A., Gilbert,D.J., Copeland,N.G. and Lowe,J.B. (1995) Molecular cloning, expression, chromosomal assignment and tissue-specific expression of a murine α- (1,3)-fucosyltransferase locus corresponding to the human ELAM-1 ligand fucosyl transferase. J. Biol. Chem., 270, 25047-25056.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25047-25056
    • Gersten, K.M.1    Natsuka, S.2    Trinchera, M.3    Petryniak, B.4    Kelly, R.J.5    Hiraiwa, N.6    Jenkins, N.A.7    Gilbert, D.J.8    Copeland, N.G.9    Lowe, J.B.10
  • 8
    • 0027244101 scopus 로고
    • Purification, cloning and expression of a bovine UDP-GalNAc:polypeptide N-acetylgalactos-aminyltransferase
    • Hagen,F.K., VanWuyckhuyse,B. and Tabak,L.A. (1993) Purification, cloning and expression of a bovine UDP-GalNAc:polypeptide N-acetylgalactos-aminyltransferase. J. Biol. Chem., 268, 18960-18965.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18960-18965
    • Hagen, F.K.1    VanWuyckhuyse, B.2    Tabak, L.A.3
  • 9
    • 0031035341 scopus 로고    scopus 로고
    • The Thomsen-Friedenreich (TF) antigen: A critical review on the structural, biosynthetic and histochemical aspects of a pancarcinoma-associated antigen
    • Hanisch,F. and Baldus,S. (1997) The Thomsen-Friedenreich (TF) antigen: a critical review on the structural, biosynthetic and histochemical aspects of a pancarcinoma-associated antigen. Histol. Histopathol., 12, 263-281.
    • (1997) Histol. Histopathol. , vol.12 , pp. 263-281
    • Hanisch, F.1    Baldus, S.2
  • 10
    • 0023065281 scopus 로고
    • Glycosylation of developing human glomeruli: Lectin binding sites during cell induction and maturation
    • Holthöfer,H. and Virtanen,I. (1987) Glycosylation of developing human glomeruli: lectin binding sites during cell induction and maturation. J. Histochem. Cytochem., 35, 33-37.
    • (1987) J. Histochem. Cytochem. , vol.35 , pp. 33-37
    • Holthöfer, H.1    Virtanen, I.2
  • 11
    • 0027178358 scopus 로고
    • Isolation and expression of a cDNA clone encoding a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
    • Homa,F.L., Hollander,T., Lehman,D.J., Thomsen,D.R. and Elhammer,A.P. (1993) Isolation and expression of a cDNA clone encoding a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. J. Biol. Chem., 268, 12609-12616.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12609-12616
    • Homa, F.L.1    Hollander, T.2    Lehman, D.J.3    Thomsen, D.R.4    Elhammer, A.P.5
  • 12
    • 0028860624 scopus 로고
    • The gene encoding murine α1,3-galactosyltransferase is expressed in female germ cells but not in male germ cells
    • Johnston,D.S., Shaper,J.H., Shaper,N.L., Joziasse,D.H. and Wright,W.W. (1995) The gene encoding murine α1,3-galactosyltransferase is expressed in female germ cells but not in male germ cells. Dev. Biol., 171, 224-232.
    • (1995) Dev. Biol. , vol.171 , pp. 224-232
    • Johnston, D.S.1    Shaper, J.H.2    Shaper, N.L.3    Joziasse, D.H.4    Wright, W.W.5
  • 13
    • 0002391476 scopus 로고
    • Functional anatomy of the kidney
    • Greger,R.F., Knauf,H. and Mutschler (eds.). Springer-Verlag, Berlin
    • Kaissling,B. and Dorup,J. (1995) Functional anatomy of the kidney. In: Greger,R.F., Knauf,H. and Mutschler (eds.). Diuretics. Springer-Verlag, Berlin, pp. 1-66.
    • (1995) Diuretics , pp. 1-66
    • Kaissling, B.1    Dorup, J.2
  • 14
    • 0028978686 scopus 로고
    • Expression of Ga1β1,4GlcNAc α, 2,6-sialyltransferase and α2,6-linked sialoglycoconjugates in normal human and rat tissues
    • Kaneko,Y., Yamamoto,H., Colley,K.J. and Moskal,J.R. (1995) Expression of Ga1β1,4GlcNAc α, 2,6-sialyltransferase and α2,6-linked sialoglycoconjugates in normal human and rat tissues. J. Histochem. Cytochem., 43, 945-954.
    • (1995) J. Histochem. Cytochem. , vol.43 , pp. 945-954
    • Kaneko, Y.1    Yamamoto, H.2    Colley, K.J.3    Moskal, J.R.4
  • 15
    • 0021262325 scopus 로고
    • Identification and characterization of podocalyxin - The major sialoprotein of the renal glomerular epithelial cell
    • Kerjaschki,D., Sharky,D.J. and Farquhar,M.G. (1984) Identification and characterization of podocalyxin - the major sialoprotein of the renal glomerular epithelial cell. J. Cell Biol., 98, 1591-1596.
    • (1984) J. Cell Biol. , vol.98 , pp. 1591-1596
    • Kerjaschki, D.1    Sharky, D.J.2    Farquhar, M.G.3
  • 16
    • 0028291625 scopus 로고
    • Differential expression of five sialyltransferase genes in human tissues
    • Kitagawa,H. and Paulson,J.C. (1994) Differential expression of five sialyltransferase genes in human tissues. J. Biol. Chem., 269, 17872-17878.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17872-17878
    • Kitagawa, H.1    Paulson, J.C.2
  • 17
    • 0027742093 scopus 로고
    • The molecular and cell biology of glycosyltransferases
    • Kleene,R. and Berger,E.G. (1993) The molecular and cell biology of glycosyltransferases. Biochim. Biophys. Acta, 1154, 283-325.
    • (1993) Biochim. Biophys. Acta , vol.1154 , pp. 283-325
    • Kleene, R.1    Berger, E.G.2
  • 18
    • 0023873843 scopus 로고
    • A standard nomenclature for structures of the kidney
    • Kriz,W., Bankir,L. (1988) A standard nomenclature for structures of the kidney. Am J. Physiol., 254, F1-F8.
    • (1988) Am J. Physiol. , vol.254
    • Kriz, W.1    Bankir, L.2
  • 19
    • 0021184735 scopus 로고
    • Appearance of Helix pomatia lectin-binding sites a podocyte plasma membrane during glomerular differentiation: A quantitative analysis using the lectin-gold technique
    • Kunz,A., Brown,D. and Orci,L. (1984) Appearance of Helix pomatia lectin-binding sites a podocyte plasma membrane during glomerular differentiation: a quantitative analysis using the lectin-gold technique. Lab. Invest., 51, 317-324.
    • (1984) Lab. Invest. , vol.51 , pp. 317-324
    • Kunz, A.1    Brown, D.2    Orci, L.3
  • 20
    • 0025201788 scopus 로고
    • Polysialic acid and N-CAM in embryonic rat kidney: Mesenchymal and epithelial elements show different patterns of expression
    • Lackie,P.M., Zuber,C. and Roth,J. (1990) Polysialic acid and N-CAM in embryonic rat kidney: mesenchymal and epithelial elements show different patterns of expression. Development, 110, 933-947.
    • (1990) Development , vol.110 , pp. 933-947
    • Lackie, P.M.1    Zuber, C.2    Roth, J.3
  • 21
    • 0023080601 scopus 로고
    • Changes in the glycosylation pattern during embryonic development of mouse kidney as revealed with lectin conjugates
    • Laitinen,L., Virtanen,I. and Saxén,L. (1987) Changes in the glycosylation pattern during embryonic development of mouse kidney as revealed with lectin conjugates. J. Histochem. Cytochem., 35, 55-65.
    • (1987) J. Histochem. Cytochem. , vol.35 , pp. 55-65
    • Laitinen, L.1    Virtanen, I.2    Saxén, L.3
  • 22
    • 0020326214 scopus 로고
    • The cellular specificity of lectin binding in the kidney. II. A light microscopical study in the rabbit
    • LeHir,M. and Dubach,U.C. (1982) The cellular specificity of lectin binding in the kidney. II. A light microscopical study in the rabbit. Histochemistry, 74, 531-540.
    • (1982) Histochemistry , vol.74 , pp. 531-540
    • LeHir, M.1    Dubach, U.C.2
  • 23
    • 0020013686 scopus 로고
    • Binding of peanut lectin to specific epithelial cell types in the kidney
    • LeHir,M., Kaissling,B., Koeppen,B.M. and Wade, J.B. (1982) Binding of peanut lectin to specific epithelial cell types in the kidney. Am J. Physiol., 242, C117-C129.
    • (1982) Am J. Physiol. , vol.242
    • LeHir, M.1    Kaissling, B.2    Koeppen, B.M.3    Wade, J.B.4
  • 24
    • 0031777054 scopus 로고    scopus 로고
    • The expanding β4-galactosyltransferase gene family: Messages from the databanks
    • Lo,N.W., Shaper,J.H., Pevsner,J. and Shaper,N.L. (1998) The expanding β4-galactosyltransferase gene family: messages from the databanks. Glycobiology, 8, 517-526.
    • (1998) Glycobiology , vol.8 , pp. 517-526
    • Lo, N.W.1    Shaper, J.H.2    Pevsner, J.3    Shaper, N.L.4
  • 25
    • 0029854853 scopus 로고    scopus 로고
    • Complexity in O-linked oligosaccharide biosynthesis engendered by multiple polypeptide N-acetylgalactosaminyltransferases
    • Marth,J.D. (1996) Complexity in O-linked oligosaccharide biosynthesis engendered by multiple polypeptide N-acetylgalactosaminyltransferases. Glycobiology, 6, 701-705.
    • (1996) Glycobiology , vol.6 , pp. 701-705
    • Marth, J.D.1
  • 26
    • 0030612615 scopus 로고    scopus 로고
    • Expression of α1-6 fucosyltransferase in rat tissues and human cancer cell lines
    • Miyoshi,E., Uozumi,N., Noda,K., Hayashi,N., Hori,M. and Taniguchi,N. (1997) Expression of α1-6 fucosyltransferase in rat tissues and human cancer cell lines. Int. J. Cancer, 72, 1117-1121.
    • (1997) Int. J. Cancer , vol.72 , pp. 1117-1121
    • Miyoshi, E.1    Uozumi, N.2    Noda, K.3    Hayashi, N.4    Hori, M.5    Taniguchi, N.6
  • 27
    • 0028097537 scopus 로고
    • Enzymes involved in mammalian oligosaccharide biosynthesis
    • Natsuka,S. and Lowe,J.B. (1994) Enzymes involved in mammalian oligosaccharide biosynthesis. Curr. Opin. Struct. Biol., 4, 683-691.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 683-691
    • Natsuka, S.1    Lowe, J.B.2
  • 28
    • 0024364391 scopus 로고
    • Tissue specific expression of sialyltransferases
    • Paulson,J., Weinstein,J. and Schauer,A. (1989) Tissue specific expression of sialyltransferases. J. Biol. Chem., 264, 10931-10934.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10931-10934
    • Paulson, J.1    Weinstein, J.2    Schauer, A.3
  • 29
    • 0024431691 scopus 로고
    • Glycosyltransferases. Structure, localization and control of cell type-specific glycosylation
    • Paulson,J.C. and Colley,K.J. (1989) Glycosyltransferases. Structure, localization and control of cell type-specific glycosylation. J. Biol. Chem., 164, 17615-17618.
    • (1989) J. Biol. Chem. , vol.164 , pp. 17615-17618
    • Paulson, J.C.1    Colley, K.J.2
  • 30
    • 0015179314 scopus 로고
    • Morphological and histochemical aspects of glycoproteins at the surface of animal cells
    • Rambourg,A. (1971) Morphological and histochemical aspects of glycoproteins at the surface of animal cells. Int. Rev. Cytol., 31, 57-114.
    • (1971) Int. Rev. Cytol. , vol.31 , pp. 57-114
    • Rambourg, A.1
  • 31
    • 0013872364 scopus 로고
    • Presence of a "cell coat" rich in carbohydrates at the surface of cells in the rat
    • Rambourg,A., Neutra,M. and Leblond,C.P. (1966) Presence of a "cell coat" rich in carbohydrates at the surface of cells in the rat. Anat. Rec., 154, 41-72.
    • (1966) Anat. Rec. , vol.154 , pp. 41-72
    • Rambourg, A.1    Neutra, M.2    Leblond, C.P.3
  • 32
    • 0025619831 scopus 로고
    • Carbohydrate histochemistry of epithelial glycoproteins
    • Graumann,W., Heitz,P.U., Lojda,Z., Pearse,A.G.E. and Schiebler,T.H. (eds.), Gustav Fischer Verlag, Stuttgart
    • Reid,P.E. and Park,C.M. (1990) Carbohydrate histochemistry of epithelial glycoproteins. In: Graumann,W., Heitz,P.U., Lojda,Z., Pearse,A.G.E. and Schiebler,T.H. (eds.), Progress in Histochemistry and Cytochemistry. Gustav Fischer Verlag, Stuttgart, pp. 1-170.
    • (1990) Progress in Histochemistry and Cytochemistry , pp. 1-170
    • Reid, P.E.1    Park, C.M.2
  • 33
    • 0024978529 scopus 로고
    • Isolation and characterization of amaranthin, a lectin present in the seeds of Amaranthus caudatus, which recognizes the T- (or cryptic T) antigen
    • Rinderle,S.J., Goldstein,I.J., Matta,K.L. and Ratcliffe,R.M. (1989) Isolation and characterization of amaranthin, a lectin present in the seeds of Amaranthus caudatus, which recognizes the T- (or cryptic T) antigen. J. Biol. Chem., 264, 16123-16131.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16123-16131
    • Rinderle, S.J.1    Goldstein, I.J.2    Matta, K.L.3    Ratcliffe, R.M.4
  • 34
    • 0025245801 scopus 로고
    • Physicochemical properties of amaranthin, the lectin from Amaranthus caudatus seeds
    • Rinderle,S.J., Goldstein,I.J. and Remsken,E.E. (1990) Physicochemical properties of amaranthin, the lectin from Amaranthus caudatus seeds. Biochemistry, 29, 10555-10561.
    • (1990) Biochemistry , vol.29 , pp. 10555-10561
    • Rinderle, S.J.1    Goldstein, I.J.2    Remsken, E.E.3
  • 35
    • 0008409728 scopus 로고
    • The lectins. Molecular probes in cell biology and membrane research
    • Roth,J. (1978) The lectins. Molecular probes in cell biology and membrane research. Exp. Pathol. Suppl., 3, 1-186.
    • (1978) Exp. Pathol. Suppl. , vol.3 , pp. 1-186
    • Roth, J.1
  • 36
    • 0024376736 scopus 로고
    • Postembedding labeling on Lowicryl K4M tissue sections: Detection and modification of cellular components
    • Tartakoff,A.M. (eds.), Academic Press, San Diego
    • Roth,J. (1989) Postembedding labeling on Lowicryl K4M tissue sections: detection and modification of cellular components. In: Tartakoff,A.M. (eds.), Methods in Cell Biol., Academic Press, San Diego, pp. 513-551,
    • (1989) Methods in Cell Biol. , pp. 513-551
    • Roth, J.1
  • 37
    • 0029763134 scopus 로고    scopus 로고
    • Glycosylation in the endoplasmic reticulum and the Golgi apparatus and cell type-specificity of cell surface glycoconjugate expression: Analysis by the protein A-gold and lectin-gold techniques
    • Roth,J. (1996) Glycosylation in the endoplasmic reticulum and the Golgi apparatus and cell type-specificity of cell surface glycoconjugate expression: analysis by the protein A-gold and lectin-gold techniques. Histochem. Cell Biol., 106, 79-92.
    • (1996) Histochem. Cell Biol. , vol.106 , pp. 79-92
    • Roth, J.1
  • 38
    • 0001553369 scopus 로고    scopus 로고
    • Topography of glycosylation in the Golgi apparatus
    • Berger,E.G. and Roth,J. (eds.), Birkhäuser, Basel
    • Roth,J. (1997) Topography of glycosylation in the Golgi apparatus. In Berger,E.G. and Roth,J. (eds.), The Golgi Apparatus. Birkhäuser, Basel, pp. 131-161.
    • (1997) The Golgi Apparatus , pp. 131-161
    • Roth, J.1
  • 39
    • 0020515436 scopus 로고
    • Regional distribution of N-acetyl-D-galactosamine residues in the glycocalyx of glomerular podocytes
    • Roth,J., Brown,D. and Orci,L. (1983) Regional distribution of N-acetyl-D-galactosamine residues in the glycocalyx of glomerular podocytes. J. Cell Biol.,96, 1189-1196.
    • (1983) J. Cell Biol. , vol.96 , pp. 1189-1196
    • Roth, J.1    Brown, D.2    Orci, L.3
  • 40
    • 0022343674 scopus 로고
    • Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus cisternal stack that may function in glycosylation
    • Roth,J., Taatjes,D., Lucocq,J., Weinstein,J. and Paulson,J. (1985) Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus cisternal stack that may function in glycosylation. Cell, 43, 287-295.
    • (1985) Cell , vol.43 , pp. 287-295
    • Roth, J.1    Taatjes, D.2    Lucocq, J.3    Weinstein, J.4    Paulson, J.5
  • 41
    • 0011579661 scopus 로고
    • Polysialic acid units are spatially and temporally expressed in developing postnatal rat kidney
    • Roth,J., Taatjes,D.J., Bitter-Suermann,D. and Finne,J. (1987) Polysialic acid units are spatially and temporally expressed in developing postnatal rat kidney. Proc. Natl Acad. Sci. USA, 84, 1969-1973.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 1969-1973
    • Roth, J.1    Taatjes, D.J.2    Bitter-Suermann, D.3    Finne, J.4
  • 42
    • 0001643589 scopus 로고
    • Biosynthesis of glycoproteins: Formation of O-linked oligosaccharides
    • Ginsberg,V. and Robbins,P.W. (eds.). John Wiley & Sons, New York
    • Sadler,J.E. (1984) Biosynthesis of glycoproteins: formation of O-linked oligosaccharides. In: Ginsberg,V. and Robbins,P.W. (eds.). Biology of Carbohydrates. John Wiley & Sons, New York, pp. 199-288.
    • (1984) Biology of Carbohydrates , pp. 199-288
    • Sadler, J.E.1
  • 44
    • 0025310584 scopus 로고
    • Expression patterns of the T antigen and the cryptic T antigen in rat fetuses: Detection with the lectin Amaranthin
    • Sata,T., Zuber,C., Rinderle,S.J., Goldstein,I.J. and Roth,J. (1990) Expression patterns of the T antigen and the cryptic T antigen in rat fetuses: detection with the lectin Amaranthin. J. Histochem. Cytochem., 38, 763-774.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 763-774
    • Sata, T.1    Zuber, C.2    Rinderle, S.J.3    Goldstein, I.J.4    Roth, J.5
  • 45
    • 0019837156 scopus 로고
    • Cytochemistry of cell glycoconjugates
    • Graumann,W., Pierce,A.G.E. and Schiebler,T.H. (eds.), Gustav Fischer Verlag, Stuttgart
    • Schrevel,J., Gros,D. and Monsigny,M. (1981) Cytochemistry of cell glycoconjugates. In: Graumann,W., Pierce,A.G.E. and Schiebler,T.H. (eds.), Progress in Histochemistry and Cytochemistry. Gustav Fischer Verlag, Stuttgart, pp. 1-269.
    • (1981) Progress in Histochemistry and Cytochemistry , pp. 1-269
    • Schrevel, J.1    Gros, D.2    Monsigny, M.3
  • 46
    • 0021223036 scopus 로고
    • Histochemical localization of sialoglyco-conjugates with a sialic acid-specific lectin from the slug Limax flavus
    • Schulte,B.A., Spicer,S.S. and Miller,R.L. (1984) Histochemical localization of sialoglyco-conjugates with a sialic acid-specific lectin from the slug Limax flavus. Histochem. J., 16, 1125-1132.
    • (1984) Histochem. J. , vol.16 , pp. 1125-1132
    • Schulte, B.A.1    Spicer, S.S.2    Miller, R.L.3
  • 48
    • 0021806048 scopus 로고
    • A new method of preparing gold probes for multiple labeling cytochemistry
    • Slot,J.W. and Geuze,H.J. (1985) A new method of preparing gold probes for multiple labeling cytochemistry. Eur. J. Cell Biol., 38, 87-93.
    • (1985) Eur. J. Cell Biol. , vol.38 , pp. 87-93
    • Slot, J.W.1    Geuze, H.J.2
  • 50
    • 0019785678 scopus 로고
    • Variability of cell surface glycoconjugates. Relation to differences in cell function
    • Spicer,S.S., Baron,D.S., Sato,A. and Schulte,B.A. (1981) Variability of cell surface glycoconjugates. Relation to differences in cell function. J. Histochem. Cytochem., 29, 994-1002.
    • (1981) J. Histochem. Cytochem. , vol.29 , pp. 994-1002
    • Spicer, S.S.1    Baron, D.S.2    Sato, A.3    Schulte, B.A.4
  • 51
    • 0028824558 scopus 로고
    • T and Tn pancarcinoma markers: Autoantigenic adhesion molecules in pathogenesis, prebiopsy carcinoma-detection and long-term breast carcinoma immunotherapy
    • Springer,G.F. (1995) T and Tn pancarcinoma markers: autoantigenic adhesion molecules in pathogenesis, prebiopsy carcinoma-detection and long-term breast carcinoma immunotherapy. Crit. Rev. Oncog., 6, 57-85.
    • (1995) Crit. Rev. Oncog. , vol.6 , pp. 57-85
    • Springer, G.F.1
  • 52
    • 0023747362 scopus 로고
    • Elderberry bark lectin-gold techniques for the detection of Neu5Ac (α2,6)Gal/GalNAc sequences: Applications and limitations
    • Taatjes,D.J., Roth,J., Peumans,W. and Goldstein,I.J. (1988) Elderberry bark lectin-gold techniques for the detection of Neu5Ac (α2,6)Gal/GalNAc sequences: applications and limitations. Histochem. J., 20, 478-490.
    • (1988) Histochem. J. , vol.20 , pp. 478-490
    • Taatjes, D.J.1    Roth, J.2    Peumans, W.3    Goldstein, I.J.4
  • 53
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin,H., Staehelin,T. and Gordon,J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA, 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 54
    • 0029758363 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of sialyltransferases
    • Tsuji,S. (1996) Molecular cloning and functional analysis of sialyltransferases. J. Biochem. (Tokyo), 120, 1-13.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 1-13
    • Tsuji, S.1
  • 57
    • 0028803582 scopus 로고
    • Purification and cDNA cloning of a human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
    • White,T., Bennett,E.P., Takio,K., Sorensen,T., Bonding,N. and Clausen,H. (1995) Purification and cDNA cloning of a human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J. Biol. Chem., 270, 24156-24165.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24156-24165
    • White, T.1    Bennett, E.P.2    Takio, K.3    Sorensen, T.4    Bonding, N.5    Clausen, H.6
  • 58
    • 0029952844 scopus 로고    scopus 로고
    • Unique genomic structure and expression of the mouse α2,8-sialyltransferase (ST8Sia III) gene
    • Yoshida,Y., Kurosawa,N., Kanematsu,T., Taguchi,A., Anta,M., Kojima,N. and Tsuji,S. (1996) Unique genomic structure and expression of the mouse α2,8-sialyltransferase (ST8Sia III) gene. Glycobiology, 6, 573-580.
    • (1996) Glycobiology , vol.6 , pp. 573-580
    • Yoshida, Y.1    Kurosawa, N.2    Kanematsu, T.3    Taguchi, A.4    Anta, M.5    Kojima, N.6    Tsuji, S.7
  • 60
    • 0004336924 scopus 로고    scopus 로고
    • Blot analysis with lectins for the evaluation of glycoproteins in cultured cells and tissues
    • Rhodes,J.M. and Milton,J.D. (eds.). Humana Press, Totowa, NJ
    • Zuber,C., Li,W.-P. and Roth,J. (1998) Blot analysis with lectins for the evaluation of glycoproteins in cultured cells and tissues. In Rhodes,J.M. and Milton,J.D. (eds.). Methods in Molecular Biology Series. Humana Press, Totowa, NJ, pp. 159-166.
    • (1998) Methods in Molecular Biology Series , pp. 159-166
    • Zuber, C.1    Li, W.-P.2    Roth, J.3


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