Tissue transglutaminase (TG2) can modify proteins by transamidation or deamidation of
specific glutamine residues. TG2 has a major role in the pathogenesis of celiac disease as it
is both the target of disease-specific autoantibodies and generates deamidated gliadin
peptides that are recognized by CD4+, DQ2-restricted T cells from the celiac lesions.
Capillary electrophoresis with fluorescence-labeled gliadin peptides was used to separate
and quantify deamidated and transamidated products. In a competition assay, the affinity of …