textjournal article
Proteomic Analysis of Lupin Seed Proteins To Identify Conglutin β as an Allergen, Lup an 1
Abstract
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 β, a major storage protein, as an allergen in seeds of Lupinus angustifolius and Lupinus albus. Purification of conglutin β 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 β, suggesting this protein is a major allergen for lupin. The L. angustifolius conglutin β allergen has been designated Lup an 1 by the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee- Text
- Journal contribution
- Biophysics
- Biochemistry
- Medicine
- Microbiology
- Cell Biology
- Genetics
- Molecular Biology
- Pharmacology
- Biotechnology
- Immunology
- Developmental Biology
- Cancer
- Inorganic Chemistry
- Hematology
- Plant Biology
- Environmental Sciences not elsewhere classified
- Biological Sciences not elsewhere classified
- Chemical Sciences not elsewhere classified
- lupin proteins
- Immunological Societies
- protein content
- angustifolius flour
- serum IgE
- International Union
- mass spectrometry
- anticholesterolemic properties
- storage protein
- 1 Lupin products
- Lupin Seed Proteins
- Identify Conglutin β
- Proteomic Analysis
- Western blots
- Lupinus albus
- conglutin β
- IgE binding
- allergen nomenclature subcommittee
- angustifolius conglutin β allergen
- Lupinus angustifolius
- IUIS