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A 50 kDa Maize γ-Zein has marked cross-reactivity with the almond major protein.

Lee, S.-H., M. Benmoussa, S.K. Sathe, K.H. Roux, S.S. Teuber, B.R. Hamaker, 2005. A 50 kDa Maize γ-Zein has marked cross-reactivity with the almond major protein. J Agric Food Chem. 53:7965-7970.

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.