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Agglutinating activity of gliadin-derived peptides from bread wheat: implications for coeliac disease pathogenesis

Auricchio, S.; De Ritis, G.; De Vincenzi, M.; Mancini, E.; Minetti, M.; Sapora, O.; Silano, V.

Biochemical and Biophysical Research Communications 121(2): 428-433

1984

ISSN/ISBN: 0006-291X
PMID: 6547342
Document Number: 240278
The PT only and cell agglutination induced by bread wheat gliadin peptides was inhibited by each of these 3 saccharides. Not only was mannan the most active saccharide in preventing cell agglutination induced by bread wheat gliadin peptides, but it was also able to dissociate agglutinated cells. As compared to the PT-digest of whole bread wheat gliadin, the digest obtained from purified A-gliadin was 10-fold more active. The PT-digest of durum wheat gliadin did not show any agglutinating activity.

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