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4.
Food Chem ; 183: 58-63, 2015 Sep 15.
Artículo en Inglés | MEDLINE | ID: mdl-25863610

RESUMEN

Mustard is a condiment added to a variety of foodstuffs and a frequent cause of food allergy. A new strategy for the detection of mustard allergen in food products is presented. The methodology is based on liquid chromatography analysis coupled to mass spectrometry. Mustard allergen Sin a 1 was purified from yellow mustard seeds. Sin a 1 was detected with a total of five peptides showing a linear response (lowest LOD was 5ng). Sin a 1 was detected in mustard sauces and salty biscuit (19±3mg/kg) where mustard content is not specified. Sin a 1, used as an internal standard, allowed quantification of this mustard allergen in foods. A novel LC/MS/MS SRM-based method has been developed to detect and quantify the presence of mustard. This method could help to detect mustard allergen Sin a 1 in processed foods and protect mustard-allergic consumers.


Asunto(s)
Antígenos de Plantas/análisis , Cromatografía Liquida/métodos , Análisis de los Alimentos/métodos , Espectrometría de Masas/métodos , Planta de la Mostaza/química , Proteínas de Plantas/análisis , Antígenos de Plantas/inmunología , Hipersensibilidad a los Alimentos/inmunología , Planta de la Mostaza/inmunología , Proteínas de Plantas/inmunología
5.
Mol Nutr Food Res ; 57(12): 2245-52, 2013 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-23983075

RESUMEN

SCOPE: Today, about 2-8% of the population of Western countries exhibits some type of food allergy whose impact ranges from localized symptoms confined to the oral mucosa to severe anaphylactic reactions. Consumed worldwide, lettuce is a Compositae family vegetable that can elicit allergic reactions. To date, however, only one lipid transfer protein has been described in allergic reaction to lettuce. The aim of this study was to identify potential new allergens involved in lettuce allergy. METHODS AND RESULTS: Sera from 42 Spanish lettuce-allergic patients were obtained from patients recruited at the outpatient clinic. IgE-binding proteins were detected by SDS-PAGE and immunoblotting. Molecular characterization of IgE-binding bands was performed by MS. Thaumatin was purified using the Agilent 3100 OFFGEL system. The IgE-binding bands recognized in the sera of more than 50% of patients were identified as lipid transfer protein (9 kDa), a thaumatin-like protein (26 kDa), and an aspartyl protease (35 and 45 kDa). ELISA inhibition studies were performed to confirm the IgE reactivity of the purified allergen. CONCLUSION: Two new major lettuce allergens-a thaumatin-like protein and an aspartyl protease-have been identified and characterized. These allergens may be used to improve both diagnosis and treatment of lettuce-allergic patients.


Asunto(s)
Alérgenos/aislamiento & purificación , Proteasas de Ácido Aspártico/inmunología , Hipersensibilidad a los Alimentos/inmunología , Lactuca/inmunología , Proteínas de Plantas/inmunología , Adulto , Alérgenos/inmunología , Secuencia de Aminoácidos , Proteasas de Ácido Aspártico/aislamiento & purificación , Reacciones Cruzadas/inmunología , Electroforesis en Gel de Poliacrilamida , Femenino , Humanos , Immunoblotting/métodos , Inmunoglobulina E/metabolismo , Masculino , Persona de Mediana Edad , Datos de Secuencia Molecular , Peso Molecular , Proteínas de Plantas/aislamiento & purificación , Prunus/inmunología , Adulto Joven
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