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  • 1
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford BSL : Blackwell Science Ltd
    Clinical & experimental allergy 30 (2000), S. 0 
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Allergy to plant-derived fresh foods has often been reported in geographical areas where birch or ragweed pollens are frequent and has been attributed to cross-reactivity to pollens.〈section xml:id="abs1-2"〉〈title type="main"〉ObjectiveThe aim of this study has been to evaluate allergy to plant-derived fresh foods among pollen-allergic patients from a birch and ragweed-free area.〈section xml:id="abs1-3"〉〈title type="main"〉MethodsNinety-five pollen-allergic patients took part in the study. The study consisted of a questionnaire, skin prick tests and challenge tests. Pollen skin tests to five grasses, eight trees and seven weeds were performed in duplicate. Prick tests (prick by prick) and challenge tests were carried out with the fresh foods.〈section xml:id="abs1-4"〉〈title type="main"〉ResultsMost patients allergic to pollens were sensitized to grass (Lolium and Phleum; 97.9%), followed by tree (Olea; 82.1%) and weed pollens (Plantago; 64.2%). 35 of the 95 pollen-allergic patients had positive skin test responses to some plant-derived fresh foods, the highest percentage corresponding to several fruits in the Rosaceae family (peach and pear, 26.3%), followed by Cucurbitacea fruits (melon, 13.7%). The 21.05% of the pollen-allergic patients were allergic to some type of plant-derived fresh food. Peach was the plant-derived fresh food which most frequently elicited allergy symptoms (12.6%), followed by melon (7.36%). The cluster of positive responses to Rosaceae fruits was higher for skin testing than for challenge testing.〈section xml:id="abs1-5"〉〈title type="main"〉ConclusionPeach was the most important allergy provoking fruit in a birch and ragweed free-area where apples were consumed at a rate of two times more than peaches and the patients allergic to pollen were principally sensitized to grass pollens.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science, Ltd
    Clinical & experimental allergy 31 (2001), S. 0 
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: There are some contradicting data about clinical allergic cross-reactivity to cephalosporins among patients who have had a previous allergic reaction to penicillins.The purpose of this study was to assess the safety of administering cephalosporins to penicillin-allergic patients.The diagnosis of penicillin allergy was made by positive skin tests to penicillin reagents and/or provocation tests with the penicillin suspected of causing the allergic reaction. To assess the clinical tolerance to cephalosporins, 41 well-characterized penicillin allergic patients diagnosed by positive skin tests and/or provocation tests were challenged with three cephalosporins that do not share the same side chain to the penicillin that induced the reactions: cephazoline, cefuroxime and ceftriaxone.Skin prick and intradermal tests with all cephalosporins tested were negative. All penicillin-allergic patients tolerated therapeutic doses of the three cephalosporins tested (cephazoline, cefuroxime and ceftriaxone) without any ill effect.These results indicate that the risk of suffering from an allergic reaction on administering cephalosporins to penicillin-allergic patients seems to be very low, provided that cephalosporins with a different side chain to the penicillin responsible for the allergic reaction are used.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background Allergenic components in melon extracts have not been described in spite of the fact that melon (Cucumis melo) is a frequent allergy-eliciting fruit. The aim of this study was to evaluate allergenic components in melon extract and to report the identification of cucumisin as a major melon allergen.Materials and methods Sera from 35 patients allergic to melon were selected on the basis of clinical symptoms, skin prick tests and oral challenge test. Allergenic components were detected by sodium dodecyl sulphate polyacrylamide gel electrophoresis and immunoblotting. Molecular characterization of IgE-binding bands was performed by N-terminal amino acid sequencing.Results More than 10 IgE-binding bands, between 10 and 80 kDa, were identified in melon extract. Out of them, four IgE-binding bands were major allergens: 14 kDa, 36 kDa, 54 kDa and 67 kDa. These major allergens, except 14 kDa band, showed the same N-terminal sequence: T-T-R-S-W-D-F-L. Research conducted with protein databases identified this N-terminal sequence as cucumisin, an alkaline serine protease, which shares structural homology with microbial subtilisin. The molecular mass of the identified bands corresponds with different molecular forms of cucumisin produced during the processing or degradation of the enzyme: 67 kDa native cucumisin, 54 kDa mature cucumisin and 36 kDa NH2-terminal cucumisin fragment.Conclusion Cucumisin (Cuc m 1) and several N-terminal cucumisin fragments are the major allergens of melon. The ubiquitous distribution of this protein family (cucumisin-like proteases) in many plant species and its high structural similarity suggest its potential role as a new panallergen in plant foods.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background: Chicken serum albumin (α-livetin) has been implicated as the causative allergen of the bird-egg syndrome. However, the clinical relevance of sensitization to this allergen has not been confirmed by specific challenge tests and environmental sampling. We investigated whether chicken albumin can be detected in air samples collected in a home with birds, and whether sensitization to this protein may cause respiratory and food allergy symptoms. The heat resistance of chicken albumin and the possible cross-reactivity with conalbumin were also investigated. Methods: We studied eight patients with food allergy to egg yolk who also suffered from respiratory symptoms (rhinitis and/or asthma) caused by exposure to birds. Sensitization to egg yolk and bird antigens was investigated by skin and serologic tests. Hypersensitivity to chicken albumin was confirmed by specific bronchial, conjunctival, and oral provocation tests. Results: All patients had positive skin tests and serum IgE against egg yolk, chicken serum, chicken meat, bird feathers, and chicken albumin. The presence of airborne chicken albumin in the domestic environment was confirmed. Specific bronchial challenge to chicken albumin elicited early asthmatic responses in six patients with asthma. An oral challenge with chicken albumin provoked digestive and systemic allergic symptoms in the two patients challenged. IgE reactivity to chicken albumin was reduced by 88% after heating at 90°C for 30 min. ELISA inhibition demonstrated only partial cross-reactivity between chicken albumin and conalbumin. Conclusions: Chicken albumin (Gal d 5) is a partially heat-labile allergen that may cause both respiratory and food-allergy symptoms in patients with the bird-egg syndrome.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Munksgaard International Publishers
    Allergy 57 (2002), S. 0 
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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