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  • 1
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background:  Food allergy to wheat induces different symptoms as atopic eczema/dermatitis syndrome (AEDS), urticaria and more severe reactions as wheat-dependent exercise-induced anaphylaxis (WDEIA). Different gliadin classes are involved in this allergy but IgE-binding epitopes are known only on ω5-gliadins and for WDEIA cases.Objectives:  The aim of the study was to identify IgE-binding epitopes on several gliadin classes and for several patients with different symptoms and ages.Methods:  Eleven sera were analysed by pepscan with overlapping synthetic peptides.Results:  Sera from five patients with anaphylaxis, urticaria or WDEIA, displayed strong IgE-binding to sequential epitopes of the repetitive domains of αβ, γ, ω2 or ω5-gliadins with two immunodominant epitopes on ω5-gliadin and a consensus motif of the type QQX1PX2QQ (X1 being L, F, S or I and X2 Q, E or G). One patient allergic to deamidated wheat proteins also had IgE to a repetitive peptide of γ and ω2-gliadins of the type QPQQPFP. Sera from four patients with AEDS detected no linear epitopes on gliadins, despite the fact that they contained specific IgE to α, β, γ or ω-gliadins. One child with AEDS recognized cysteine-containing sequences in the nonrepetitive domains of αβ and γ-gliadins.Conclusion:  B epitopes in wheat allergy were different from B epitopes of coeliac disease. Differences exist in IgE-binding epitopes between patients with food allergy to wheat. IgE from those suffering from WDEIA, anaphylaxis and urticaria detected sequential epitopes in the repetitive domain of gliadins whereas IgE from AEDS patients probably recognized conformational epitopes.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Screening a human small intestinal library with human serum yielded a clone which encoded a protein res4-22 the gene of which was highly homologous to a recently described gene located in the Huntington's disease locus. Autoantibodies against res4-22 (anti-res4-22), mainly of the immunoglobulin (Ig)A type, were detected in patients with neurological disorders at a higher frequency (18.4%) than in healthy blood donors (8.0%). In neurological patients with cerebral ischaemia anti-res4-22 was found significantly more often (47.4%) than in the total group of neurological patients. Anti-res4-22 positive sera showed significantly more frequently myelin staining in cerebellum and nerve sections than anti-res4-22 negative sera. Our findings demonstrate a new species of human autoantibodies against a newly described protein the function of which is still unknown.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Basis of Disease 1181 (1993), S. 169-173 
    ISSN: 0925-4439
    Keywords: Coeliac disease ; Gliadin peptide ; Peptide ; Toxicity, in vitr
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    European food research and technology 210 (1999), S. 93-96 
    ISSN: 1438-2385
    Keywords: Key words Gliadin components ; Toxicity ; Coeliac disease ; Foetal intestine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Although gliadins are known to induce coeliac disease, the toxicity of single gliadin components is still uncertain. Therefore, the main components of ω-, α- and γ-type gliadins from the wheat cultivar Rektor were preparatively separated by RP-HPLC. Purity and type of the isolated components (one ω-, eight α- and four γ-gliadins) were confirmed by N-terminal amino acid sequencing. Gliadin components were digested with immobilised pepsin and trypsin and 0.5 mg of dialysed hydrolysates was tested with a foetal chick intestine assay which has been proven to be specific for the coeliac toxic effect of total gliadin and enzymatic hydrolysates. The reduction in sucrase activity was compared with a control culture and was taken as an indicator for toxicity. The results demonstrated that all the gliadin components studied remarkably reduced the increase in sucrase activity to 23–68% of the control assays. Important differences in the inhibitory action between the three gliadin types could not be detected, and only in a few cases did the single components differ significantly. Based on these results, it seems impossible to remove the toxic factor of gliadins by plant breeding.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-2013
    Keywords: Monosaccharide absorption ; Small intestine ; Vascular perfusion ; Unstirred layers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Na dependence ofd-glucose and 3-O-methyl-d-glucose absorption was investigated using the isolated rabbit small intestine perfused through the lumen and the vascular bed, thus imitating in vivo conditions. No dependence of monosaccharide transport on luminal Na concentration was demonstrable if the lumen was perfused at low flow rate. Due to Na secretion, however, Na concentration in the lumen bulk phase, initially being zero, was raised to more than 20 mmol/l during the course of the experiments. Na dependence of sugar transport could be shown, however, if (1) Na secretion was decreased (by use of a vascular medium with low Na concentration) or if (2) unstirred layer thickness was reduced (by enhancement of luminal flow rate). Both conditions allowed the Na concentration near the brush border membrane to be controlled. The results provide an experimental explanation for the apparently low degree of Na dependence of monosaccharide absorption under in vivo conditions.
    Type of Medium: Electronic Resource
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