Identification of a monoclonal antibody to abscission tissue that recognizes xylose/fucose-containing N-linked oligosaccharides from higher plants

Monoclonal antibodies raised against extracts of the rachis abscission zone of Sambucus nigra L. were selected for high reactivity towards abscission-zone proteins. One antibody (YZ1/2.23) has been shown to cross-react, by both indirect and competition enzyme-linked immunosorbent assay and by Wester...

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Veröffentlicht in:Planta 1988-10, Vol.175 (4), p.506-512
Hauptverfasser: McManus, M.T. (London Univ., Egham, Surrey (UK). Royal Holloway and Bedford New Coll., Dept. of Biochemistry), McKeating, J, Secher, D.S, Osborne, D.J, Ashford, D, Dwek, R.A, Rademacher, T.W
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Sprache:eng
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Zusammenfassung:Monoclonal antibodies raised against extracts of the rachis abscission zone of Sambucus nigra L. were selected for high reactivity towards abscission-zone proteins. One antibody (YZ1/2.23) has been shown to cross-react, by both indirect and competition enzyme-linked immunosorbent assay and by Western blotting, with a number of plant enzymes including horseradish peroxidase, rice α-glucosidase, almond β-glucosidase and the lectins from Phaseolus vulgaris and Erythrina cristagalli. The major N-linked oligosaccharide isolated from horseradish peroxidase has the sequence Manα3(Manα6)(Xylβ2)Manβ4GlcNAcβ4(Fucα3) GlcNAc. This oligosaccharide was found to be a potent inhibitor of the binding of YZ1/2.23 to the intact glycoprotein. The common determinant is therefore contained within this structure.
ISSN:0032-0935
1432-2048
DOI:10.1007/BF00393072