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Characterization of antigens from the human exocrine pancreatic tissue (Pag) relevant as target antigens for autoantibodies in Crohn's disease
Author(s) -
Harald Fricke,
Andreas Birkhofer,
C Folwaczny,
W Meister,
Scriba Pc
Publication year - 1999
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1046/j.1365-2362.1999.00414.x
Subject(s) - autoantibody , pancreas , glycoprotein , antigen , ammonium , ammonium sulfate precipitation , immunofluorescence , chemistry , biochemistry , indirect immunofluorescence , salt (chemistry) , microbiology and biotechnology , biology , antibody , size exclusion chromatography , immunology , enzyme , organic chemistry
Background The present study was performed to analyse the immunological properties of the autoantigens recognized by autoantibodies against exocrine pancreas (PAb), which have been described in Crohn's disease. Methods Autoantibodies were detected by indirect immunofluorescence. Inhibition studies were performed by preincubating tissue sections with various glycoproteins and the different fractions obtained in fractioned salt precipitation of pancreas homogenate with ammonium sulphate. Immunoblotting of human pancreas homogenate was conducted using PAb‐positive sera. Results In size exclusion chromatography, the molecular weight of the pancreas autoantigen (PAg) was determined as > 800 kD. In the fractionated salt precipitation, the autoantigen could be detected in fractions I (0–25% ammonium sulphate) and III (50–90% ammonium sulphate). In immunoblotting, a number of protein bands were observed (at 16, 18, 19, 24, 27, 29, 31 and 34 kD), and the binding pattern showed little variation between individual patients. Conclusions The protein that is recognized by PAb appears to be a large protein complex consisting of several subunits which exhibit reactivity to PAb.