
This work was aimed to study the patterns of zein glycosylation. Zein proteins included 1-3% of sugars. The affinity of different lectins, such as concanavalin A (Con A), Lens culinaris lectin (LCL) and lectins of Arachis hypogaea (PNA), of Triticum vulgaris (WGA), of Dolichos biflorus (DBA), of Glycin max (SBA), of Lotus tetragonolobus (LTA), of Laburnum anagiroides (LAL), of Ricinus communis (RCA), of Phaseolus vulgaris (PHA) was used to analyze the glycosylation sites. All selected lectins interacted with zein proteins. It may serve a basis for determination of mannose, galactose, fucose and aminosugars. Some lectins were bound only by prolamines of some inbred lines, while others were connected with all lines.
Glycosylation, Zein, Carbohydrates, Proteins, Zea mays, Lectins, Seeds, Carbohydrate Metabolism, Drug Interactions, Electrophoresis, Polyacrylamide Gel, Plant Lectins, Plant Proteins, Prolamins, Protein Binding
Glycosylation, Zein, Carbohydrates, Proteins, Zea mays, Lectins, Seeds, Carbohydrate Metabolism, Drug Interactions, Electrophoresis, Polyacrylamide Gel, Plant Lectins, Plant Proteins, Prolamins, Protein Binding
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