Abstract
Monoclonal IgM with anti-Pr2 activity was purified from the serum of a patient with chronic cold agglutinin disease. After reduction with 20 mM dithiothreitol IgM molecules and J chains were separated. The subunits were reoxidized in the presence and in the absence of J chains. In both mixtures cold agglutinin activity against the Pr2 antigen was restored to the titre of the native IgM. Complement fixation as measured by the C1 fixation and transfer test was recovered in the reassociated materials no matter whether J chains were present or not. It was concluded that the presence of J chains was not required for antigen binding and complement fixing activity of IgM antibodies.
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