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A reaction is described between some streptococci and IgA myeloma proteins; most streptococci showed low affinity for IgA myeloma proteins, with the exception of group A, type M 4 and two freshly isolated group A streptococci; they took up 40 to 50 per cent of 1 μg 125I labelled IgA myeloma protein added. Addition of similar amounts of unlabelled IgA and IgG myeloma proteins showed no cross inhibition between uptake of IgG and IgA. Heat‐ and trypsin treatment of the streptococci did not reveal any differences in IgA and IgG reactivity. The uptake of one 125 I labelled IgA myeloma protein was inhibited uniformely by four randomly selected unlabelled IgA myeloma proteins. Thus, the uptake of 125 I labelled IgA myeloma protein seems to be independent from the specificity of the antibody combining sites.
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Christensen et al. (1975) studied this question.
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