Development of a novel C1q immunoadsorbent for removal of circulating immunecomplexes: quantitative isolation of hepatitis B virus surface antigen and immunecomplexes |
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Authors: | Y Gazitt S Margel A Lerner J R Wands D Shouval |
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Affiliation: | 1. Department of Molecular Biology, Hebrew University — Hadassah Medical School, Jerusalem, Israel;2. Department of Plastics Research, Weizmann Institute of Science, Rehovot, Israel;3. Liver Unit, Department of Medicine A, Hadassah University Hospital, Jerusalem, Israel;4. Gastrointestinal Unit, Massachussetts General Hospital, Boston, MA, U.S.A. |
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Abstract: | A technique for large scale production of human C1q from plasma by affinity chromatography on an anti-C1q column is described. Affinity purified C1q was covalently coupled to a newly developed agarose polyacrolein microsphere beads immunoadsorbent. This immunoadsorbent was utilized for quantitative removal of artificially formed bovine serum albumin (BSA)-anti-BSA immune complexes (IC). The C1q affinity column was then used for the isolation of immunecomplexes containing hepatitis B virus (HBV) surface antigen (HBsAg) from serum of an HBsAg carrier. Identical columns may be utilized for quantitative removal of a variety of IC from blood of patients with infectious and autoimmune diseases, as well as neoplastic diseases. Furthermore, dissociated immunecomplexes will provide an additional source for purification of specific antigens. |
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Keywords: | affinity purification HBsAg immune complex C1q |
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