SEPARATION OF CELIAC-ACTIVE PEPTIDES FROM BREAD WHEAT WITH THE AID OF METHYLPYRROLIDINONE CHITOSAN

Gliadin-derived peptides from haxaploid wheat, known to be toxic for in-vitro cultured small-intestinal mucosa from coeliac patients, are very active in agglutinating K562(S) cells. Chromatographic data obtained with the use of methylpyrrolidinone chitosan coupled to Sepharose-6B indicate that a minor (1.3%) fraction of the peptides binds very strongly to the support at nearly neutral pH values, and can be eluted at pH 2.85. This fraction is the one responsible for the agglutination of K562(S) cells, being one-hundred times more active than the digest from which it has been separated.