Purification and characterisation of antigenic gliadins in coeliac disease

Two gliadins, known to be especially antigenic in coeliac disease, were purified to homogeneity by a series of ion-exchange chromatography steps. Their N-terminal amino acid sequences showed minor differences but clearly classified them as gamma-type gliadins. The purified gliadins were further characterised with respect to amino acid composition, molecular mass and E1(1%)cm at 276 nm. Based on these properties it is suggested that one of them is identical to a gamma-type gliadin, earlier characterised by its nucleotide sequence, whereas the other has not previously been described. The purification procedure may form the basis for the development of a more differentiated analysis of circulating antibodies for diagnosis and makes clinical testing of the toxicity of defined gliadin peptides feasible.