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

McManus MT., McKeating J., Secher DS., Osborne DJ., Ashford D., Dwek RA., Rademacher TW.

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 Manα 3(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.

DOI

10.1007/bf00393072

Type

Journal article

Publication Date

1988-10-01T00:00:00+00:00

Volume

175

Pages

506 - 512

Total pages

6

Addresses

Department of Biochemistry, Royal Holloway and Bedford New College, University of London, TW20 0EX, Egham, Surrey, UK.

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