{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,2,8]],"date-time":"2025-02-08T05:24:16Z","timestamp":1738992256971,"version":"3.37.0"},"reference-count":40,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"5","license":[{"start":{"date-parts":[[2015,9,1]],"date-time":"2015-09-01T00:00:00Z","timestamp":1441065600000},"content-version":"tdm","delay-in-days":9254,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["lww.com","ovid.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1990,5]]},"abstract":"<jats:sec>\n            <jats:title\/>\n            <jats:p>In normal individuals there is an adaptive immune response to a foreign antigen in which antibodies of increasing affinity are produced with time. This is not always true of an autoimmune response. However, because only a limited number of autoantigens have been cloned or purified, this issue has not been studied well. In primary biliary cirrhosis the predominant manifestation of autoimmunity is antimitochondrial antibodies that react with dihydrolipoamide transacetylase. The availability of recombinant dihydrolipoamide transacetylase and the develoopment of a rapid and reproducible enzyme\u2013linked immunosorbent assay for autoantibodies has allowed us to address the affinity of autoantibodies using thiocyanate inhibition. Thiocyanate is a chaotropic compound known to inhibit antigen\u2013antibody binding in a concentration\u2013dependent manner. We used this property to inhibit the binding by enzyme\u2013linked immunosorbent assay of human recombinant dihydrolipoamide transacetylase with serum autoantibodies from 55 patients with primary biliary cirrhosis. The relative affinity and serum autoantibody titers were then compared with the histological stage of the liver biopsy sample. Interestingly, we found a considerable heterogeneity of relative affinities. These relative affinities did not correlate with the histological stage or the serum titer of antimitochondrial antibodies. However, the ability of serum autoantibodies to inhibit intact primary biliary cirrhosis enzyme activity was found to correlate highly (R<jats:sup>2<\/jats:sup> = 0.751) with the relative affinity. Thus there are profound differences between patients with respect to qualitative expression of autoantibodies. The significance of this data will be unclear until more is determined regarding the nature of the epitope that drives T cells and leads to B\u2013cell responses.(HEPATOLOGY 1990; 11:717\u2013722.)<\/jats:p>\n          <\/jats:sec>","DOI":"10.1002\/hep.1840110502","type":"journal-article","created":{"date-parts":[[2007,3,3]],"date-time":"2007-03-03T23:27:36Z","timestamp":1172964456000},"page":"717-722","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":10,"title":["The Relative Affinity of Recombinant Dihydrolipoamide Transacetylase for Autoantibodies in Primary Biliary Cirrhosis"],"prefix":"10.1097","volume":"11","author":[{"given":"Craig A.","family":"Robertson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ross L.","family":"Coppel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thomas","family":"Prindiville","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David","family":"Fregeau","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marshall","family":"Kaplan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rolland E.","family":"Dickson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eric M.","family":"Gershwin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"276","reference":[{"key":"10.1002\/hep.1840110502-BIB1","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/0022-1759(86)90268-1","volume":"86","author":"Pullen","year":"1986","journal-title":"J Immunol Methods"},{"key":"10.1002\/hep.1840110502-BIB2","first-page":"1","volume-title":"Advances in immunoly","volume":"10","author":"Siskind","year":"1969","unstructured":". Cell selection by antigen in the immune response. In: , eds. Advances in immunoly. Vol 10. New York: Academic Press, 1969: 1\u201345."},{"key":"10.1002\/hep.1840110502-BIB3","first-page":"145","volume-title":"Antibody affinity: thermodynamic aspects and biological signifiance","author":"Steward","year":"1983","unstructured":". Antibody affinity: thermodynamic aspects and biological signifiance. 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