Abstract
The reactivity of native IgM anti-B and of the monomer subunits with B cells was investigated using 125I-labelled antibody. A proportion of the monomers produced by mercaptoethanol treatment retained antibody activity, but the value of the equilibrium constant of the subunits was reduced by a factor of 36–170 compared to that of the native IgM molecule. It is concluded that native IgM anti-B is attached to red cells by at least two combining sites and evidence is given which indicates that IgM anti-A behaves similarly.
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Selected References
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