Epitopes recognised by tissue transglutaminase antibodies in coeliac disease.
作者： Ken Nakachi , Michael Powell , Gillian Swift , Marie-Andrée Amoroso , Rossitza Ananieva-Jordanova
DOI: 10.1016/J.JAUT.2003.09.002
关键词:
摘要: Abstract The interaction between IgA tissue transglutaminase (tTG) antibodies (Abs) and 35 S-labelled tTG produced in a transcription/translation (TnT) system with various amino acid (aa) deletions has been studied. These experiments showed that the N-terminal aa 1–89 were important for Ab binding all 15 coeliac disease sera studied central residues (aa 401–491) of Abs but one sera. contribution C-terminal to varied different overall was less than contributions N terminal regions. Mouse monoclonal (MAbs) sequences recognised by MAbs determined using modified proteins. Analysis inhibiting effects patient on confirmed importance regions forming serum sites. Recombinant human expressed yeast purified better 95% homogeneity MAb affinity chromatography as final purification step. This material highly suitable use an ELISA tTGAb.
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