Purification of Recombinant Peanut Allergen Ara h 1 and Comparison of IgE Binding to the Natural Protein

Author:

Hurlburt Barry,McBride Jane,Nesbit Jacqueline,Ruan Sanbao,Maleki Soheila

Publisher

MDPI AG

Subject

Plant Science,Health Professions (miscellaneous),Health (social science),Microbiology,Food Science

Reference23 articles.

1. Table 13 Peanut Area, Yield, and Production http://www.apps.fas.usda.gov/psdonline/psdreport.aspx?hidReportRetrievalName=BVS&hidReportRetrievalID=918&hidReportRetrievalTemplateID=1#ancor

2. US prevalence of self-reported peanut, tree nut, and sesame allergy: 11-year follow-up;Sicherer;J. Allergy Clin. Immunol.,2010

3. Mutational analysis of the IgE-binding epitopes of the peanut allergen, Ara h 3: A member of the glycinin family of seed-storage proteins;Rabjohn;J. Allergy Clin. Immun.,1999

4. Biochemical and structural analysis of the IgE binding sites on Ara h1, an abundant and highly allergenic peanut protein;Shin;J. Biol. Chem.,1998

5. Identification and mutational analysis of the immunodominant IgE binding epitopes of the major peanut allergen Ara h 2;Stanley;Arch. Biochem. Biophys.,1997

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