期刊
EUROPEAN JOURNAL OF BIOCHEMISTRY
卷 269, 期 21, 页码 5175-5181出版社
WILEY
DOI: 10.1046/j.1432-1033.2002.03215.x
关键词
autoimmunity; celiac disease; transglutaminase; epitope mapping; phage display
资金
- Telethon [E.1141] Funding Source: Medline
Celiac disease is an intestinal malabsorption characterized by an intolerance to cereal proteins accompanied by immunological responses to dietary gliadins and a autoantigen located in the endomysium. The latter has been identified as the enzyme tissue transglutaminase which belongs to a family of enzymes that catalyze protein cross-linking reactions and is constitutively expressed in many tissues as well as being activated during apoptosis. I a recent paper, we described the selection and characterization of anti-transglutaminase Igs from phage antibody libraries created from intestinal lymphocytes from celiac disease patients. In this work, using transglutaminase gene fragments, we identify a region of tissue transglutaminase recognized by these antibodies as being conformational and located in the core domain of the enzyme. This is identical to the region recognized by anti-transglutaminase Igs found in the serum of celiac disease patients.
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