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Development of a novel C1q immunoadsorbent for removal of circulating immunecomplexes: quantitative isolation of hepatitis B virus surface antigen and immunecomplexes
Authors:Y Gazitt  S Margel  A Lerner  J R Wands  D Shouval
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.
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.
Keywords:affinity purification  HBsAg  immune complex C1q
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