ISOLATION AND PURIFICATION OF INDIVIDUAL GLIADIN PROTEINS BY PREPARATIVE ACID POLYACRYLAMIDE GEL ELECTROPHORESIS (A-PAGE) FOR ALLERGENIC RESEARCH
 
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Pol. J. Food Nutr. Sci. 2007;57(1):91–96
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ABSTRACT
Gliadins are a large and complex group of proteins, consisting of dozens to hundreds of unique polypeptides in any wheat cultivar. Individual gliadins differ in molecular weight, isoelectric point, and amino acid sequences, making their analyses especially difficult. We here used preparative polyacrylamide gel electrophoresis in acidic conditions to fractionate gliadins of the cultivar Fraza. Resulting fractions were then analysed by ELISA to test their immunoreactive properties with antigliadin polyclonal antibodies. Preparative electrophoresis yielded 60 aliquots, of which 15 contained single proteins. Separated gliadins differed in immunoreactive properties: antigliadin antibodies bound stronger to α and β gliadins, while the immunoenzymatic reaction with γ and ω-gliadins was much weaker.
ISSN:1230-0322