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Volumn 318, Issue 1-2, 2007, Pages 20-29

Development of a sensitive and reliable ELISA for quantification of wheat germ agglutinin

Author keywords

ELISA; Lectin; Pig gastric mucin; Quantification; Wheat germ agglutinin

Indexed keywords

CARBOHYDRATE; LECTIN; WHEAT GERM AGGLUTININ;

EID: 33845913755     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jim.2006.07.025     Document Type: Article
Times cited : (12)

References (17)
  • 1
    • 0027194326 scopus 로고
    • Characterisation of two different glycosylated domains from the insoluble mucin complex of rat small intestine
    • Carlstedt I., Hermann A., Karlsson H., Sheehan J., Fransson L.A., and Hansson G.C. Characterisation of two different glycosylated domains from the insoluble mucin complex of rat small intestine. J. Biol. Chem. 268 (1993) 18771
    • (1993) J. Biol. Chem. , vol.268 , pp. 18771
    • Carlstedt, I.1    Hermann, A.2    Karlsson, H.3    Sheehan, J.4    Fransson, L.A.5    Hansson, G.C.6
  • 3
    • 0036824317 scopus 로고    scopus 로고
    • An alkaline phosphatase lacking wheat germ agglutinin binding sites; useful enzyme for lectin assays with comparable activity to the calf enzyme
    • Farajollahi M.M., Cook D.B., and Self C.H. An alkaline phosphatase lacking wheat germ agglutinin binding sites; useful enzyme for lectin assays with comparable activity to the calf enzyme. Iran. Biomed. J. 6 (2002) 105
    • (2002) Iran. Biomed. J. , vol.6 , pp. 105
    • Farajollahi, M.M.1    Cook, D.B.2    Self, C.H.3
  • 4
    • 0030774645 scopus 로고    scopus 로고
    • Lectin-mediated bioadhesion: proteolytic stability and binding characteristics of wheat germ agglutinin and Solanum tuberosum lectin on Caco-2, HT-29 and human colonocytes
    • Gabor F., Wirth M., Jurkovich B., Haberl I., Theyer G., Walcher G., and Hamilton G. Lectin-mediated bioadhesion: proteolytic stability and binding characteristics of wheat germ agglutinin and Solanum tuberosum lectin on Caco-2, HT-29 and human colonocytes. J. Control. Release 49 (1997) 27
    • (1997) J. Control. Release , vol.49 , pp. 27
    • Gabor, F.1    Wirth, M.2    Jurkovich, B.3    Haberl, I.4    Theyer, G.5    Walcher, G.6    Hamilton, G.7
  • 5
    • 0034477636 scopus 로고    scopus 로고
    • Composition of N-linked carbohydrates from ovalbumin and co-purified glycoproteins
    • Harvey D.J., Wing D.R., Küster B., and Wilson I.B.H. Composition of N-linked carbohydrates from ovalbumin and co-purified glycoproteins. J. Am. Soc. Mass Spectrom. 11 (2000) 564
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 564
    • Harvey, D.J.1    Wing, D.R.2    Küster, B.3    Wilson, I.B.H.4
  • 6
    • 0028146780 scopus 로고
    • In vitro study of lectin-latex conjugates for specific bioadhesion
    • Irache J.M., Durrer C., Duchêne D., and Ponchel G. In vitro study of lectin-latex conjugates for specific bioadhesion. J. Control. Release 31 (1994) 181
    • (1994) J. Control. Release , vol.31 , pp. 181
    • Irache, J.M.1    Durrer, C.2    Duchêne, D.3    Ponchel, G.4
  • 7
    • 0019252614 scopus 로고
    • Lectins in the Unites States diet: a survey of lectins in commonly consumed foods and a review of the literature
    • Nachbar M.S., and Oppenheim J.D. Lectins in the Unites States diet: a survey of lectins in commonly consumed foods and a review of the literature. Am. J. Clin. Nutr. 33 11 (1980) 2338
    • (1980) Am. J. Clin. Nutr. , vol.33 , Issue.11 , pp. 2338
    • Nachbar, M.S.1    Oppenheim, J.D.2
  • 8
    • 0017287098 scopus 로고
    • Transmembrane control of the receptors on normal and tumor cells: I. Cytoplasmic influence over surface components
    • Nicolson G.L. Transmembrane control of the receptors on normal and tumor cells: I. Cytoplasmic influence over surface components. Biochim. Biophys. Acta 457 (1976) 57
    • (1976) Biochim. Biophys. Acta , vol.457 , pp. 57
    • Nicolson, G.L.1
  • 9
    • 0025240776 scopus 로고
    • Role of putative "link" glycopeptide of intestinal mucin in binding of piliated Escherichia coli serotype O157:H7 strain CL-49
    • Sajjan S.U., and Forstner J.F. Role of putative "link" glycopeptide of intestinal mucin in binding of piliated Escherichia coli serotype O157:H7 strain CL-49. Infect. Immun. 58 (1990) 868
    • (1990) Infect. Immun. , vol.58 , pp. 868
    • Sajjan, S.U.1    Forstner, J.F.2
  • 10
    • 0033571597 scopus 로고    scopus 로고
    • Comparison of methods of immobilization to enzyme-linked immunosorbent assay plates for the detection of sugar chains
    • Satoh A., Fukui E., Yoshino S., Shinoda M., Kojima K., and Matsumoto I. Comparison of methods of immobilization to enzyme-linked immunosorbent assay plates for the detection of sugar chains. Anal. Biochem. 275 2 (1999) 231
    • (1999) Anal. Biochem. , vol.275 , Issue.2 , pp. 231
    • Satoh, A.1    Fukui, E.2    Yoshino, S.3    Shinoda, M.4    Kojima, K.5    Matsumoto, I.6
  • 11
    • 0017404321 scopus 로고
    • The action of proteolytic enzymes on the glycoprotein from pig gastric mucus
    • Scawen A., and Allen A. The action of proteolytic enzymes on the glycoprotein from pig gastric mucus. Biochem. J. 163 (1977) 363
    • (1977) Biochem. J. , vol.163 , pp. 363
    • Scawen, A.1    Allen, A.2
  • 12
    • 0023050165 scopus 로고
    • Carbohydrate structures of bovine submaxillary mucin
    • Tsuji T., and Osawa T. Carbohydrate structures of bovine submaxillary mucin. Carbohydr. Res. 151 (1986) 391
    • (1986) Carbohydr. Res. , vol.151 , pp. 391
    • Tsuji, T.1    Osawa, T.2
  • 13
    • 0037164034 scopus 로고    scopus 로고
    • Quantitative determination of dietary lectin activities by enzyme-linked immunosorbent assay using specific glycoproteins immobilised on microtiter plates
    • Vincenzi S., Zoccatelli G., Perbellini F., and Rizzi C. Quantitative determination of dietary lectin activities by enzyme-linked immunosorbent assay using specific glycoproteins immobilised on microtiter plates. J. Agric. Food Chem. 50 (2002) 6266
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 6266
    • Vincenzi, S.1    Zoccatelli, G.2    Perbellini, F.3    Rizzi, C.4
  • 14
    • 0026605368 scopus 로고
    • A hemagglutinating substance in chitin
    • Whitmore F.A. A hemagglutinating substance in chitin. Biotechniques 12 2 (1992) 202
    • (1992) Biotechniques , vol.12 , Issue.2 , pp. 202
    • Whitmore, F.A.1
  • 15
    • 1542363594 scopus 로고    scopus 로고
    • Interaction of bile salts with gastrointestinal mucins
    • Wiedmann T.S., Liang W., and Herrington H. Interaction of bile salts with gastrointestinal mucins. Lipids 39 1 (2004) 51
    • (2004) Lipids , vol.39 , Issue.1 , pp. 51
    • Wiedmann, T.S.1    Liang, W.2    Herrington, H.3
  • 16
    • 0032424017 scopus 로고    scopus 로고
    • Lectin-mediated drug targeting: binding capacity and uptake of wheat germ agglutinin and Solanum tuberosum lectin by Caco-2 and HT-29 cells
    • Wirth M., and Gabor F. Lectin-mediated drug targeting: binding capacity and uptake of wheat germ agglutinin and Solanum tuberosum lectin by Caco-2 and HT-29 cells. J. Drug Target. 6 (1998) 95
    • (1998) J. Drug Target. , vol.6 , pp. 95
    • Wirth, M.1    Gabor, F.2
  • 17
    • 0037133115 scopus 로고    scopus 로고
    • Lectin-mediated drug delivery: influence of mucin on cytoadhesion of plant lectins in vitro
    • Wirth M., Gerhardt K., Wurm C., and Gabor F. Lectin-mediated drug delivery: influence of mucin on cytoadhesion of plant lectins in vitro. J. Control. Release 79 (2002) 183
    • (2002) J. Control. Release , vol.79 , pp. 183
    • Wirth, M.1    Gerhardt, K.2    Wurm, C.3    Gabor, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.