MASS SPECTROMETRY AS A TOOL FOR PROBING GLUTEN PEPTIDE MODIFICATIONS RELEVANT TO CELIAC DISEASE

摘要

Transglutaminase(TG)-cataIyzed transamidation of gliadin peptic-tryptic digest has been evaluated by HPLC and nES-MS/MS analysis. By tagging with mono-dansylcadaverine (M.DC) as ucyl-acceptor, transamidalcd fluorescent peptides were identified as a/fJ-, y-gliadin, and LMW glutenin fragments. The sequence consensus for transamidation and dearnidation was Q-X-P and Q-X-Q. The benefit of the procedure lies in its vast applicability for defining Q susceptibility pathways of any dietary protein to TGase.