Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2003 Jul;112(1):175-9.
doi: 10.1067/mai.2003.1480.

Activated charcoal forms non-IgE binding complexes with peanut proteins

Affiliations

Activated charcoal forms non-IgE binding complexes with peanut proteins

Peter Vadas et al. J Allergy Clin Immunol. 2003 Jul.

Abstract

Background: Conventional management of peanut-induced anaphylaxis is composed of administration of epinephrine, antihistamine, and steroid and stabilization of airway, ventilatory, and circulatory function. Therapies directed toward slowing or preventing further absorption of peanut protein from the gastrointestinal tract after accidental ingestion have not been a routine part of management.

Objective: The purpose of this study was to determine the ability of activated charcoal to complex with peanut protein, thereby preventing its binding to either peanut-specific IgE or peanut-specific IgG.

Methods: Peanut protein was coincubated with micronized activated charcoal suspension at pH 3.5 or 7.4. Peanut protein complexed with charcoal was removed by centrifugation. Binding of residual peanut protein to peanut-specific IgG was measured by a sandwich ELISA assay. Also, ability of uncomplexed peanut protein to bind to peanut-specific IgE was determined by Western blot and by skin prick testing in subjects with peanut allergy.

Results: Activated charcoal (AC) formed complexes with peanut protein, effectively competing for binding with peanut-specific IgG in a sandwich ELISA assay. AC complexed efficiently with peanut protein at both neutral and acidic pH in as little as 60 seconds. AC was also able to remove IgE-binding peanut allergens from solution as determined by Western blot and by skin prick testing in subjects with peanut allergy. A ratio of 200 mg of AC to 1 mg peanut protein was required for complete removal of peanut protein from solution. AC was able to complex with peanut protein within food matrices such as ice cream and chocolate.

Conclusion: The data presented herein show that AC removes both IgE-binding and IgG-binding peanut proteins from solution rapidly at both neutral and acidic pH. These data suggest that administration of AC may be useful as an adjunct to slow or to prevent further absorption of peanut protein from the gastrointestinal tract after accidental ingestion by individuals with peanut allergy.

PubMed Disclaimer

Similar articles

Cited by

Publication types

MeSH terms

LinkOut - more resources