We reported a rare case of hyperviscosity syndrome with IgA
1-λ type M protein. Hyperviscosity was due to complex formation between patient's abnormal IgA
1 and fibrinogen. Gel formation of patient's plasma occurred during withdrawal of venous blood. The α
1 heavy and λ light chains of this purified abnomal IgA
1 were found to have the same molecular weight as the normal IgA. Isoelectric points of abnormal α
1 heavy chain ranged from 4.6 to 5.2 which were changed toward the neutral pH upon treatment with sialidase. Since the complex formation was reversible depending upon the temperature, the association between abnormal IgA
1 and fibrinogen seems to be noncovalent. As a result of analysis of amino acid sequence, 16th amino acid of CH
1 domain changed to cystein from tyrosine. These data suggest that amino acid sequence or abnormality of second structure in the variable region of patient's IgA differs from that of nomal IgA, and that these abnormalities are concerned with association with fibrinogen.
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