A study of the sites of glycosylation of zein proteins using the lectin concanavalin A |
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Authors: | JA Smith WL Rottmann I Rubenstein |
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Institution: | 1. Department of Horticultural Sciences and Landscape Architecture University of Minnesota, St. Paul, MN 55108 U.S.A.;2. Department of Genetics and Cell Biology, University of Minnesota, St. Paul, MN 55108 U.S.A. |
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Abstract: | The sites of glycosylation of zeins, the maize (Zea mays L.) storage proteins, were studied using the affinity of the lectin Concanavalin A (Con A) for certain glycosides. Zeins which were extracted from kernels of Illinois High Protein (IHP), W22, W64A and Oh43 were separated by isoelectric focusing and analyzed with a radiolabeled Con A binding technique. Certain sub-groups of the zein proteins contained carbohydrate moities which bound Con A while others did not. Zeins extracted from Oh43 kernels had a higher relative affinity for Con A than those of other maize lines. Further analyses of the zeins of Oh43 by gas chromatography demonstrated the presence of fucose, mannose and glucose. |
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Keywords: | zeins glycosylation Concanavalin A Con A Concanavalin A IEF isoelectric focusing IHP Illinois High Protein SDS sodium dodecyl sulfate |
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