Abstract
Abstract The M-components of two macroglobulinemia sera were found to consist of two (serum Naae) and four (serum To) species of IgMK immunoglobulins on the basis of differences in charge, solubility properties, antipolysaccharide specificity or avidity, individual antigenic specificity, amino acid composition of light chains, and NH2-terminal amino acid sequences of light or heavy chains. Striking structural similarities were apparent between individual species of each set of M-components, such as sharing of antipolysaccharide specificity (M-components Naae), and individual antigenic specificity. Furthermore, the light and heavy chains of each set belonged to the same V-region subgroups, and all the To kappa chain species (VkIII) had Val in Position 2. One of the Nae heavy chains (VhIII) had Asp in Position 6, indicating that it represented an unusual VhIII variant. One of the M-components reacted with a human cartilage proteoglycan, probably a chondroitin sulphate-protein complex. The data suggest that antigenic selection may be involved in the development of this limited heterogeneity.
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