Home | My Profile | Contact Us
Research Trends Products  |   order gateway  |   author gateway  |   editor gateway  
Register | Forgot Password

Author Resources
 Author Gateway
 Article submission guidelines

Editor Resources
 Editor/Referee Gateway

 Regional Subscription Agents/Distributors
Current Trends in Immunology   Volumes    Volume 18 
Identification of the water-soluble protein components with acidic and neutral pHi in peanuts and determination of their immunoreactivity and behavior under roasting
Imène Boualeg, Aissa Boutebba, Paulo Marcelo
Pages: 29 - 41
Number of pages: 13
Current Trends in Immunology
Volume 18 

Copyright © 2017 Research Trends. All rights reserved

Peanuts contain many proteins, some of which may cause adverse immunological reactions in atopic individuals. In this study, the main functional compounds of the water-soluble fraction of peanut seeds were identified using ultra performance liquid chromatography (UPLC) separation coupled with high resolution mass spectrometry (Orbitrap). Using two- and one-dimensional electrophoresis, it was revealed that the raw peanut seeds extract contains several protein components of pHi between 3 and 7 and of different molecular weights. IgE immunoreactivity of a patient allergic to this food, realized by 1D western blot analysis, allowed for the detection of allergens. The 1D electrophoresis of the isolated substance of peanuts roasted at 140 °C for 40 min showed roasting-resistant components. Mass spectrometry allowed us to detect the monomeric form of the allergen Ara h1 (conarachin) and its isoforms (P41B and P17). For the allergens Ara h3, Ara h2 and Ara h6 several protein entities were identified: Ara h3/Ara h4, Gly 1, a storage protein, glycinin and arachin Ahy-3 OS for Ara h3, and conglutin-7 for Ara h2 and conglutin for Ara h6. These molecular entities were characterized by a low molecular weight of 16.9 to 71.3 kDa and acidic or neutral pHi. The immunoblotting indicated that the isoform P41B and conarachin were sources of allergy. Specific epitopes were detected: NNFGKLFEVK and NEGVIVKSKEHVEELTKHAKSVSK for the isoform P41B, SSDNEGVIVK for conarachin and REREEDWRQP for the isoform P41B and conarachin. Glycinin (Ara h3) and conglutin (Ara h6) were resistant to heat treatment, unlike the isoform P17 and conglutin-7 (Ara h2) which were relatively sensitive to this treatment.
Buy this Article


Buy this article
Buy this volume
Subscribe to this title
Shopping Cart

Quick Links
Search Products
Browse in Alphabetical Order : Journals
Browse by Subject Classification : Journals

Ordering Information Ordering Information
Downloadable forms Downloadable Forms