Journal of Agricultural and Food Chemistry · 2008 · 89 citations · 29 references
Life SciencesBiochemistryImmunologyAllergyFood AnalysisProteomicsFood AllergensFood AllergyIge-mediated AllergyProtein AnalysisProtein CharacterizationSeed ProteomicsAllergen NomenclatureFood AllergenicityMass Spectrometry ProteomicsMolecular Basis Of AllergenicityNomenclatureProteomic ClassificationProteomic Data AnalysisSeed Protein Extraction
Lupin products may be valuable as human foods because of their high protein content and potential anticholesterolemic properties. However, a small percentage of the population is allergic to lupin. In this study, we use in vitro IgE binding and mass spectrometry to identify conglutin beta, a major storage protein, as an allergen in seeds of Lupinus angustifolius and Lupinus albus. Purification of conglutin beta from L. angustifolius flour confirmed that serum IgE binds to this protein. Where IgE in sera recognized lupin proteins on Western blots, it recognized conglutin beta, suggesting this protein is a major allergen for lupin. The L. angustifolius conglutin beta allergen has been designated Lup an 1 by the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations