IgE-Binding Proteins in Almonds (Prunus amygdalus); Identification by Immunoblotting with Sera from Almond-Allergic Adults

Authors

  • T.RACY J. BARGMAN,

    1. Authors Rupnow and Taylor are with the Dept. of Food Science & Technology, Food Industry Complex, Univ. of Nebraska, Lincoln, NE 68583–0919. Author Bergman's present affiliation: General Mills, Inc., James Ford Bell Technical Center, 9000 Plymouth Avenue N., Minneapolis, MN 55427.
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  • J.OHN H. RUPNOW,

    1. Authors Rupnow and Taylor are with the Dept. of Food Science & Technology, Food Industry Complex, Univ. of Nebraska, Lincoln, NE 68583–0919. Author Bergman's present affiliation: General Mills, Inc., James Ford Bell Technical Center, 9000 Plymouth Avenue N., Minneapolis, MN 55427.
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  • S.TEVE L. TAYLOR

    1. Authors Rupnow and Taylor are with the Dept. of Food Science & Technology, Food Industry Complex, Univ. of Nebraska, Lincoln, NE 68583–0919. Author Bergman's present affiliation: General Mills, Inc., James Ford Bell Technical Center, 9000 Plymouth Avenue N., Minneapolis, MN 55427.
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  • Paper No.9768, Journal Series, Nebraska Agricultural Experiment Station. We are grateful to the Institute of Food Technologists Fellowship Committee for the support Tracy Bargman received during her graduate program.

ABSTRACT

The allergenicity of three raw almond varieties (Nonpareil, Mission and Carmel) and three types of processed almonds (blanched, blanched-roasted, and almond butter) were examined and compared by immunoblotting using sera eight almond-allergic individuals. Serum from the 8 individuals exhibited unique IgE-binding patterns with most of the binding activity occurring with proteins of molecular weights between 30,000 and 70,000 daltons. Two major allergens were identified with molecular weights of ca 70,000 and 45,000–50,000 daltons, with each of these proteins binding to sera from 4 of the 8 allergic individuals. The immunoreactivity of the larger one was reduced by heat processing, while the smaller one was not affected.

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