Matches in SemOpenAlex for { <https://semopenalex.org/work/W1569885244> ?p ?o ?g. }
Showing items 1 to 25 of
25
with 100 items per page.
- W1569885244 abstract "L’allergie a l’arachide represente un tiers des allergies alimentaires en France. Elle entraine des reactions souvent severes et ne s’attenue que rarement avec l’âge. Elle releve principalement d’une reaction d’hypersensibilite immediate mediee par les immunoglobulines de type E (IgE) specifiques de certaines proteines de l’arachide. De nombreuses proteines et fragments peptidiques extraits de la graine, purifies par chromatographies et caracterises par sequencage ainsi que par analyse proteomique, ont pu etre classes dans trois familles de proteines de reserve des plantes, les globulines 7S, 11S et les albumines 2S. L’etude de la capacite de liaison aux IgE de ces proteines et des peptides qui en derivent a ete menee a l’aide de 80 serums de patients allergiques a l’arachide par des techniques de type ELISA. Des allergenes majeurs (entrainant une reponse IgE specifique intense chez la majorite des patients) se retrouvent dans chacune des familles. Les albumines 2S presentent le potentiel allergenique le plus marque. Chaque patient est sensibilise a plusieurs proteines. De plus, pour chaque allergene, les IgE peuvent reconnaitre plusieurs regions intramoleculaires. Selon les proteines, les differents traitements thermiques peuvent modifier ou non le potentiel allergenique. Les processus digestifs realises in vivo et dans des tests de digestibilite in vitro degradent completement les proteines mais ne suppriment pas le potentiel allergenique de l’arachide. Les fragments peptidiques de faible masse moleculaire tels que ceux issus de ces hydrolyses enzymatiques jouent vraisemblablement un role important dans la mise en place et le developpement de l’allergie a l’arachide.________________________________________________________________________________________________________Peanut allergy represents about 30% of food allergies in France. It is one of the most frequent cause of severe food-associated anaphylaxis and it tends to persist throughout life. Allergy to peanut is an IgE-mediated reaction. Several proteins and peptide fragments derived therefrom were extracted from the kernels. They were purified by a combinaison of selective precipitations and chromatographic separations, then characterized by N-terminal amino acid sequencing and proteomics. They belong to 3 major plant storage protein families, i.e. the 7S and 11S globulins and 2S albumins. The analysis of the IgE-binding capacity of those proteins and derived peptides was performed by Enzyme AllergoSorbent Test (EAST) and EAST inhibition using the sera of 80 peanut allergic patients. The major allergens which lead to an intense specific IgE response in the vast majority of patients were found in each plant protein family. 2S albumins exhibited the most important allergenic potential. Each patient appeared to be sensitized to numerous proteins. Moreover, for each allergen, several intramolecular regions were recognized by specific IgE. Depending on the allergen, the different thermal processings either modified or did not modify the allergenic potential. Proteins were extensively degraded during in vivo and in vitro digestion but their allergenic potential was not abolished. Low molecular weight peptide fragments such as those formed by pepsin and pepsin, trypsin and chymotrypin hydrolysis certainly play a central role in the sensitization process and the development of peanut allergy." @default.
- W1569885244 created "2016-06-24" @default.
- W1569885244 creator A5027245152 @default.
- W1569885244 date "2005-07-12" @default.
- W1569885244 modified "2023-09-27" @default.
- W1569885244 title "Diversité de la réponse IgE dans l'allergie à l'arachide : caractérisation des allergènes et devenir de leur potentiel allergénique lors des traitements thermiques et des processus digestifs" @default.
- W1569885244 hasPublicationYear "2005" @default.
- W1569885244 type Work @default.
- W1569885244 sameAs 1569885244 @default.
- W1569885244 citedByCount "2" @default.
- W1569885244 crossrefType "dissertation" @default.
- W1569885244 hasAuthorship W1569885244A5027245152 @default.
- W1569885244 hasConcept C153911025 @default.
- W1569885244 hasConcept C185592680 @default.
- W1569885244 hasConcept C86803240 @default.
- W1569885244 hasConceptScore W1569885244C153911025 @default.
- W1569885244 hasConceptScore W1569885244C185592680 @default.
- W1569885244 hasConceptScore W1569885244C86803240 @default.
- W1569885244 hasLocation W15698852441 @default.
- W1569885244 hasOpenAccess W1569885244 @default.
- W1569885244 hasPrimaryLocation W15698852441 @default.
- W1569885244 isParatext "false" @default.
- W1569885244 isRetracted "false" @default.
- W1569885244 magId "1569885244" @default.
- W1569885244 workType "dissertation" @default.