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Identification of a Specific IgE‐Binding Protein from Narrow‐Leafed Lupin ( L. Angustifolius ) Seeds
Author(s) -
Kłos Patrycja,
Poręba Elżbieta,
Springer Ewa,
LampartSzczapa Eleonora,
Józefiak Anna Goździcka
Publication year - 2010
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2009.01440.x
Subject(s) - lupinus angustifolius , globulin , western blot , immunoglobulin e , lupinus , protein subunit , chemistry , allergen , allergy , biochemistry , biology , botany , immunology , antibody , gene
Since lupin has been introduced as a food ingredient on the market there are more and more reports concerning its allergenic properties. However, only few narrow‐leafed lupin proteins have yet been characterized as specific IgE‐binding molecules and identified. The aim of the study has been to find and identify the main narrow‐leafed lupin globulins that bind to specific IgEs from the sera of lupin‐allergic people. Isolated lupin globulins were subjected to immunoblotting with the sera from people who suffered from lupin allergy. Incubation with α‐methyl‐D‐galactopyranoside was performed to eliminate possible binding of unspecific human IgEs. The proteins binding specific IgEs from lupin‐allergic patients' sera were identified by means of mass spectrometry. Western blot analysis revealed 2 signals corresponding to lupin globulins that bound to specific IgEs from the sera of people allergic to lupin. The globulins were identified as conglutin‐γ and its smaller subunit. The results suggested that individuals that displayed lupin allergy symptoms reacted to conglutin‐γ. Practical Application: The results of the study can contribute to identification of yet undetected allergens of narrow‐leafed lupin. This, in turn, can make lupin‐fortified products safer for the consumers.