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Evans, S.A., Olson, S.T., and Shore, J.D. (1982) p-Aminobenzamidine as a Fluorescent Probe for the Active Site of Serine Proteases. Journal of Biological Chemistry, 257, 3014-3017.

has been cited by the following article:

  • TITLE: Peanut Allergens Attached with p-Aminobenzamidine Are More Resistant to Digestion than Native Allergens

    AUTHORS: Si-Yin Chung, Shawndrika Reed, Dunhua Zhang

    KEYWORDS: p-Aminobenzamidine, Peanut Allergens, Ara h 1 and Ara h 2, Resistance to Digestion

    JOURNAL NAME: Food and Nutrition Sciences, Vol.7 No.14, December 5, 2016

    ABSTRACT: Despite being known as resistant proteins, peanut allergens (Ara h 1 and Ara h 2) can be digested and cause allergic reactions. Making the allergens more resistant to digestion may aid in non-absorption and excretion of the allergens. Our objectives were to make Ara h 1 and Ara h 2 more resistant to digestion and test them in a model system using trypsin as the digestive enzyme. The resistant allergens were prepared by covalently attaching p-aminobenzamidine (pABA), a protease inhibitor, to peanut allergens in an extract or on a PVDF membrane using glutaraldehyde, and were then tested for resistance to trypsin digestion. SDS-PAGE and Western blot were performed to determine the allergenic capacity of the modified allergens. A control was prepared using glycine instead. Results showed that Ara h 2, when covalently attached with pABA, was more resistant to trypin digestion than the native allergen. Similarly, Ara h 1, prepared on a PVDF membrane and treated with pABA, displayed a resistance to trypsin digestion. Treatment of the allergens with glycine (a control) instead of pABA showed that the modified allergens were as digestible as native allergens. Blot assays showed that the pABA-treated allergens exhibited a lower allergenic capacity than native allergens. It was concluded that pABA, when attached to peanut allergen Ara h 1 or Ara h 2, inhibited digestion of the allergen by trypsin and reduced their allergenic capacity as well.