The variable regions of cold agglutinins with anti-I and anti-Pr specificities were investigated by N-terminal amino acid sequencing and by analyses of pyrrolidonecarboxylic acid-blocked peptides after digestion of polypeptide chains with Nargase. Results showed that the heavy chains of four IgM anti-I cold agglutinins are exclusively VHI subgroups and their light chains are exclusively VKII subgroup. In contrast, the light chains of two cold agglutinins with anti-Pr specificity are not VKII, while their heavy chains are not restricted to a single subgroup. The amino acid sequences at the first hypervariable region of light chains (positions 25- 35) are similar in two of the four anti-I cold agglutinins. These sequences are different from that of the light chain of another cold agglutinin with anti-Pr specificity. These results support the concept that only antibodies with the same specificity can share similar primary structure at their antigen combining sites.
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