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פותח על ידי קלירמאש פתרונות בע"מ -
Vicilin and the basic subunit of legumin are putative chickpea allergens
Year:
2013
Source of publication :
Food Chemistry
Authors :
אשל, דני
;
.
טפר-במנולקר, פאולה
;
.
Volume :
138
Co-Authors:
Bar-El Dadon, S., School of Nutritional Sciences, Robert H. Smith Faculty of Agriculture, Food and Environment, University of Jerusalem, P.O. Box 12, 76100 Rehovot, Israel
Pascual, C.Y., Laboratorio de Inmunoalergia, Hospital Infantil La Paz, Castellana 261, 28046 Madrid, Spain
Eshel, D., Department of Postharvest Science, Agricultural Research Organization, Volcani Center, 50250 Bet-Dagan, Israel
Teper-Bamnolker, P., Department of Postharvest Science, Agricultural Research Organization, Volcani Center, 50250 Bet-Dagan, Israel
Paloma Ibáñez, M.D., Servicio de Alergia, Hospital Infantil Oniversitario Niño Jesús, Madrid, Spain
Reifen, R., School of Nutritional Sciences, Robert H. Smith Faculty of Agriculture, Food and Environment, University of Jerusalem, P.O. Box 12, 76100 Rehovot, Israel
Facilitators :
From page:
13
To page:
18
(
Total pages:
6
)
Abstract:
IgE-mediated reactions to food allergens constitute a major health problem in industrialized countries. Chickpea is consumed in Mediterranean countries, and reportedly associated with IgE-mediated hypersensitivity reactions. However, the nature of allergic reactions to chickpea has not been characterized. A serum pool from paediatric patients allergic to chickpeas was used to detect IgE-binding proteins from chickpea seeds by immunoassay and immunoblot inhibition assay. Protein samples enriched in chickpea legumin and vicilin were obtained by anion exchange chromatography, and were identified by mass spectrometric analysis. IgE-immunoassays of globulin fractions from chickpeas revealed that vicilin (50 kDa) and the basic subunit of legumin (20 kDa) were bound by IgE from patient sera. Pea and lentil protein extracts strongly inhibited the IgE binding to chickpea globulin. We speculate that vicilin and the basic subunit of legumin are major chickpea allergens. Also, the globulin fraction of chickpea likely cross-reacts with the allergenic proteins of pea and lentil. © 2012 Elsevier Ltd. All rights reserved.
Note:
Related Files :
anion exchange chromatography
Cicer arietinum
Female
Male
Pisum sativum
proteins
vicilin
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.foodchem.2012.10.031
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
18675
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:23
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Scientific Publication
Vicilin and the basic subunit of legumin are putative chickpea allergens
138
Bar-El Dadon, S., School of Nutritional Sciences, Robert H. Smith Faculty of Agriculture, Food and Environment, University of Jerusalem, P.O. Box 12, 76100 Rehovot, Israel
Pascual, C.Y., Laboratorio de Inmunoalergia, Hospital Infantil La Paz, Castellana 261, 28046 Madrid, Spain
Eshel, D., Department of Postharvest Science, Agricultural Research Organization, Volcani Center, 50250 Bet-Dagan, Israel
Teper-Bamnolker, P., Department of Postharvest Science, Agricultural Research Organization, Volcani Center, 50250 Bet-Dagan, Israel
Paloma Ibáñez, M.D., Servicio de Alergia, Hospital Infantil Oniversitario Niño Jesús, Madrid, Spain
Reifen, R., School of Nutritional Sciences, Robert H. Smith Faculty of Agriculture, Food and Environment, University of Jerusalem, P.O. Box 12, 76100 Rehovot, Israel
Vicilin and the basic subunit of legumin are putative chickpea allergens
IgE-mediated reactions to food allergens constitute a major health problem in industrialized countries. Chickpea is consumed in Mediterranean countries, and reportedly associated with IgE-mediated hypersensitivity reactions. However, the nature of allergic reactions to chickpea has not been characterized. A serum pool from paediatric patients allergic to chickpeas was used to detect IgE-binding proteins from chickpea seeds by immunoassay and immunoblot inhibition assay. Protein samples enriched in chickpea legumin and vicilin were obtained by anion exchange chromatography, and were identified by mass spectrometric analysis. IgE-immunoassays of globulin fractions from chickpeas revealed that vicilin (50 kDa) and the basic subunit of legumin (20 kDa) were bound by IgE from patient sera. Pea and lentil protein extracts strongly inhibited the IgE binding to chickpea globulin. We speculate that vicilin and the basic subunit of legumin are major chickpea allergens. Also, the globulin fraction of chickpea likely cross-reacts with the allergenic proteins of pea and lentil. © 2012 Elsevier Ltd. All rights reserved.
Scientific Publication
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