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Volume 270, Number 15, Issue of April 14, pp. 8571-8577, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Pak H. Poon , Sherie L. Morrison , Verne N. Schumaker

Two pairs of chimeric, domain-switched immunoglobulins with identical murine, anti-dansyl (5-dimethylaminonaphthalene-1-sulfonyl) variable domains have been generated, employing as parent antibodies a human IgM and a mouse IgG2b. The first pair of chimeric antibodies µµµ and µ was generated by switching the Cµ3 and C2 domains between IgM and IgG2b. The second pair of chimeras µµ and µµ were formed by switching both Cµ3 and Cµ4 with C2 and C3. SDS-polyacrylamide gel electrophoresis and analytical ultracentrifugation showed that over half (57 and 71%) of the two chimeric antibodies possessing the Cµ4 domain and tail piece formed disulfide-linked IgM-like polymers. In contrast, the two chimeric antibodies lacking the Cµ4 domain were almost entirely monomeric. Both monomeric chimeras had reduced ability to activate complement. The chimera µ had no activity under any of the assay conditions, whereas µµ caused only a small amount of cell lysis but was fully active in consuming complement at 4 °C. The polymeric chimera µµ was much less active than IgM, bound C1 weakly and caused some cell lysis but consumed little complement with soluble antigen. The polymeric chimera µµµ bound C1strongly and was the most active antibody in all assays, even more active than the parental IgG2b and IgM antibodies; it was the only antibody that exhibited antigen-independent activity. The results suggest that Cµ3 alone does not constitute the complement binding site in IgM but requires both Cµand Cµfor full activity.

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