A 50 kDa maize γ-zein has marked cross-reactivity with the almond major protein

Sung Ho Lee, Mustapha Benmoussa, Shridhar K. Sathe, Kenneth H. Roux, Suzanne S Teuber, Bruce R. Hamaker

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


Cross-reactivity of antibodies against almond major protein (AMP, a legumin), the major almond allergen, with cereal proteins may cause problems in detecting almond contaminants in cereal products when antibody-based assays are used. Rabbit polyclonal IgG antiserum produced against AMP was used to test cross-reactivity with protein extracts from maize, a cereal commonly found in breakfast and snack foods. Gradient SDS-PAGE followed by Western blotting was performed, and two cross-reactive proteins were detected by chemiluminescence. A fraction of maize proteins purified by elution from an IgG anti-AMP affinity column followed by electrophoreseis and immunoblotting showed a high degree of cross-reactivity with a minor 50 kDa protein of maize, as well as low cross-reactivity with the 27 kDa γ-zein. The 50 kDa cross-reactive protein was identified as the 50 kDa γ-zein by immunoreaction with anti-50 kDa γ-zein antiserum. Notably, the 50 kDa maize γ-zein also reacted with IgE from pooled human sera from patients with self-reported severe almond allergies. The high immunoreactivity of the 50 kDa γ-zein should be considered in maize quality improvement programs, and such notable cross-reactivity is of relevance in the design of antibody-based assays for almond allergen detection.

Original languageEnglish (US)
Pages (from-to)7965-7970
Number of pages6
JournalJournal of Agricultural and Food Chemistry
Issue number20
StatePublished - Oct 5 2005


  • γ-zein
  • Allergen
  • Almond major protein
  • Cross-reactivity
  • Immunoreaction
  • Maize

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Food Science
  • Chemistry (miscellaneous)


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