Multiplicity of allergens in peanuts

Barnett, D. and Baldo, B.A. and Howden, M.E.H. (1983) Multiplicity of allergens in peanuts. Journal of Allergy and Clinical Immunology, 72 (1). pp. 61-68.

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Crude protein fractions from raw and roasted groundnuts were examined in the radioallergosorbent test (RAST) with 10 serum samples from patients with clinical groundnut sensitivity. The radioactive uptake results, which were generally high, did not show any distinguishable pattern. Two commercially available groundnut proteins, groundnut lectin and phospholipase D, gave poor RAST responses. Three purified groundnut proteins, α-arachin, conarachin I and concanavalin A-reactive glycoprotein, all gave significant RAST results which were generally less than those with the crude extracts. The extent of RAST inhibition with those materials was inversely related to their abundance in the total groundnut protein. Crossed immunoelectrophoresis with extracts from raw and roasted groundnut indicated the presence of 22 and 10 anodically migrating antigens, respectively. There were 16 immunoglobulin (Ig)E binding antigens for raw groundnut and 7 for roasted groundnut after incubation with a mixed serum from the 10 patients in crossed radioimmunoelectrophoresis (CRIE) using 125I-labelled anti-IgE. CRIE plates treated with individual serum samples showed that all the patients had specific IgE for the major antigen peak, which was tentatively identified as α-arachin. That major storage protein of groundnut, which is particularly heat resistant, may be of greater clinical significance than its apparently low RAST activity would seem to indicate

Item Type: Article
Author Affiliation: School of Chemistry, Macquarie Univ., North Ryde, NSW 2113, Australia
Subjects: Plant Protection
Divisions: Groundnut
Depositing User: Mr B Krishnamurthy
Date Deposited: 31 May 2012 14:36
Last Modified: 31 May 2012 14:36

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