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• W2046219488 abstract "A variety of monoclonal antibodies was prepared to wheat (Triticum aestivum L.) gluten proteins, and their antigenic specificities were assessed using non-denaturing polyacrylamide gradient and SDS-polyacrylamide gel electrophoresis and immunoblotting techniques. While most anti-gliadin monoclonal antibodies bound to all gliadin protein bands separated by one-dimensional electrophoresis, several antibodies binding to small groups of gliadin proteins were identified. At high concentrations, these ‘specific’ antibodies bound to an increasing number of gliadins; this is likely due to the very high sequence homologies between groups of gliadin proteins. Several monoclonal antibodies with specificities for glutenin proteins were produced. These antibodies bound to all major glutenin subunits, although at low antibody concentrations some bound selectively to a single subunit. Other anti-glutenin antibodies bound to minor glutenin subunits and a variety of gliadin proteins. Several bound to gamma gliadins and high-molecular-weight glutenins, suggesting that these groups of proteins bear considerable homology. The results are reviewed in relation to known information on gluten protein structure, derived from DNA-sequencing studies." @default.
• W2046219488 created "2016-06-24" @default.
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• W2046219488 date "1986-12-01" @default.
• W2046219488 modified "2023-10-07" @default.
• W2046219488 title "Specificity characteristics of monoclonal antibodies to wheat grain storage proteins" @default.
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• W2046219488 doi "https://doi.org/10.1016/0167-4838(86)90023-3" @default.
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