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.
Sjöström
H
H
Department of Biochemistry C, Panum Institute, University of Copenhagen, Denmark.
Friis
S U
SU
Norén
O
O
Anthonsen
D
D
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000941:Antigens / Q000302:isolation & purification*; D002446:Celiac Disease / Q000276:immunology*; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D005903:Gliadin / Q000276:immunology / Q000302:isolation & purification*; D006801:Humans; D015151:Immunoblotting; D008969:Molecular Sequence Data
D000596:Amino Acids; D000941:Antigens; D005903:Gliadin