Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.10.3.3 (ascorbate oxidase)
 778 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ole e 1, the major allergen from olive pollen, is a glycoprotein containing a single Asn-linked glycan moiety. Rabbit antiserum against this protein has been obtained; and its immunologic cross-reactivities in Western blotting with ascorbate oxidase, horseradish peroxidase, bromelain, ovalbumin, and honeybee venom phospholipase A2 have been studied. Ascorbate oxidase, peroxidase, and bromelain are recognized by the Ole e 1 antiserum. When these three proteins are deglycosylated by periodate treatment, such an immunologic reaction does not occur. The relative affinities of these proteins have been analyzed by direct and inhibition ELISA experiments. A commercially available antibody against horseradish peroxidase has also been considered in these studies. This antibody reacts with Ole e 1 but not with the periodate-deglycosylated allergen. Horseradish peroxidase, bromelain, and ascorbate oxidase are recognized by the IgE of sera from patients who are hypersensitive to olive tree pollen. This binding is also abolished by periodate treatment. The results are interpreted in terms of the presence of an epitope in the carbohydrate moiety of Ole e 1, which would contain a xylose involved in recognition by both IgE and IgG antibodies.
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PMID:Cross-reactivity between the major allergen from olive pollen and unrelated glycoproteins: evidence of an epitope in the glycan moiety of the allergen. 864 22

The binding to concanavalin A (Con A) by pyridylaminated oligosaccharides derived from bromelain (Manalpha1,6(Xylbeta1,2) Manbeta1, 4GlcNAcbeta1,4(Fucalpha1,3)GlcNAc), horseradish peroxidase (Manalpha1,6(Manalpha1,3) (Xylbeta1,2)Manbeta1, 4GlcNAcbeta1,4(Fucalpha1,3) GlcNAc), bee venom phospholipase A2 (Manalpha1,6Manbeta1,4GlcNAcbeta1,4GlcNAc and Manalpha1,6(Manalpha1,3)Manbeta1,4GlcNAcbeta1,4 (Fucalpha1,3)GlcNAc) and zucchini ascorbate oxidase (Manalpha1,6(Manalpha1,3) (Xylbeta1,2)Manbeta1,4 GlcNAcbeta1,4GlcNAc) was compared to the binding by Man3GlcNAc2, Man5GlcNAc2 and the asialo-triantennary complex oligosaccharide from bovine fetuin. While the fetuin oligosaccharide did not bind, bromelain, zucchini, Man2GlcNAc2 and horseradish peroxidase were retarded (in that order). The alpha1,3-fucosylated phospholipase, Man3GlcNAc2 and Man5GlcNAc2 structures were eluted with 15 mM alpha-methylmannoside. It is concluded that core alpha1,3-fucosylation has little or no effect on ConA binding while xylosylation decreases affinity for ConA. In a parallel study comparing the endoglycosidase D (Endo D) sensitivities of Man3GlcNAc2, IgG-derived GlcNAcbeta1, 2Manalpha1,6(GlcNAcbeta1,2Manalpha1,3)Manbeta1,+ ++4GlcNAcbeta1,4(Fucalpha1,6)GlcNAc, the phospholipase Manalpha1,6(Manalpha1,3) Manbeta1, 4GlcNAcbeta1,4(Fucalpha1,3)GlcNAc, and horseradish and zucchini pyridylaminated N-linked oligosaccharides, it was found that only the Man3GlcNAc2 structure was cleaved. The IgG structure was sensitive only when beta-hexosaminidase was also present. Thus, in contrast to core alpha1,6-fucosylated structures, such as those present in mammals, the presence of core alpha1,3-fucose, as found in structures from plants and insects, and/or beta1,2-xylose, as found in plants, causes resistance to Endo D.
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PMID:Concanavalin A binding and endoglycosidase D resistance of beta1,2-xylosylated and alpha1,3-fucosylated plant and insect oligosaccharides. 955 83